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Article ; Online: Stiffness-dependent motility and proliferation uncoupled by deletion of CD44.

Razinia, Ziba / Castagnino, Paola / Xu, Tina / Vázquez-Salgado, Alexandra / Puré, Ellen / Assoian, Richard K

2017 Volume 7, Issue 1, Page(s) 16499

Abstract: Information in the microenvironment guides complex cellular decisions such as whether or not to proliferate and migrate. The effects of soluble extracellular signals on these cellular functions are fairly well understood, but relatively little is known ... ...

Abstract	Information in the microenvironment guides complex cellular decisions such as whether or not to proliferate and migrate. The effects of soluble extracellular signals on these cellular functions are fairly well understood, but relatively little is known about how the extracellular matrix (ECM), and particularly the mechanical information in the ECM, guides these cellular decisions. Here, we show that CD44, a major receptor for the glycosaminoglycan ECM component hyaluronan, coordinates the motility and proliferative responses to ECM stiffening. We analyzed these cellular responses on fibronectin-coated polyacrylamide hydrogels prepared at a physiologic range of ECM stiffness and found that stiffening of the ECM leads to both cell cycling and cell motility in serum-stimulated primary mouse dermal fibroblasts. Remarkably, deletion of CD44 impaired stiffness-stimulated motility of the primary cells without affecting other hallmark cellular responses to ECM stiffening including cell spread area, stress fiber formation, focal adhesion maturation, and intracellular stiffening. Even stiffness-mediated cell proliferation was unaffected by deletion of CD44. Our results reveal a novel effect of CD44, which is imposed downstream of ECM-mechanosensing and determines if cells couple or uncouple their proliferative and motility responses to ECM stiffness.
MeSH term(s)	Animals ; Biomarkers ; Cell Movement/genetics ; Cell Proliferation ; Cell Shape ; Cellular Microenvironment ; Extracellular Matrix/metabolism ; Fibroblasts ; Gene Deletion ; Hyaluronan Receptors/genetics ; Male ; Mechanotransduction, Cellular ; Mice ; Mice, Knockout ; Phosphorylation
Chemical Substances	Biomarkers ; Hyaluronan Receptors
Language	English
Publishing date	2017-11-28
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-017-16486-z
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Article ; Online: ASB2α, an E3 ubiquitin ligase specificity subunit, regulates cell spreading and triggers proteasomal degradation of filamins by targeting the filamin calponin homology 1 domain.

Razinia, Ziba / Baldassarre, Massimiliano / Cantelli, Gaia / Calderwood, David A

The Journal of biological chemistry

2013 Volume 288, Issue 44, Page(s) 32093–32105

Abstract: Filamins are actin-binding and cross-linking proteins that organize the actin cytoskeleton and anchor transmembrane proteins to the cytoskeleton and scaffold signaling pathways. During hematopoietic cell differentiation, transient expression of ASB2α, ... ...

Abstract	Filamins are actin-binding and cross-linking proteins that organize the actin cytoskeleton and anchor transmembrane proteins to the cytoskeleton and scaffold signaling pathways. During hematopoietic cell differentiation, transient expression of ASB2α, the specificity subunit of an E3-ubiquitin ligase complex, triggers acute proteasomal degradation of filamins. This led to the proposal that ASB2α regulates hematopoietic cell differentiation by modulating cell adhesion, spreading, and actin remodeling through targeted degradation of filamins. Here, we show that the calponin homology domain 1 (CH1), within the filamin A (FLNa) actin-binding domain, is the minimal fragment sufficient for ASB2α-mediated degradation. Combining an in-depth flow cytometry analysis with mutagenesis of lysine residues within CH1, we find that arginine substitution at each of a cluster of three lysines (Lys-42, Lys-43, and Lys-135) renders FLNa resistant to ASB2α-mediated degradation without altering ASB2α binding. These lysines lie within previously predicted actin-binding sites, and the ASB2α-resistant filamin mutant is defective in targeting to F-actin-rich structures in cells. However, by swapping CH1 with that of α-actinin1, which is resistant to ASB2α-mediated degradation, we generated an ASB2α-resistant chimeric FLNa with normal subcellular localization. Notably, this chimera fully rescues the impaired cell spreading induced by ASB2α expression. Our data therefore reveal ubiquitin acceptor sites in FLNa and establish that ASB2α-mediated effects on cell spreading are due to loss of filamins.
MeSH term(s)	Animals ; CHO Cells ; Cricetinae ; Cricetulus ; Filamins/genetics ; Filamins/metabolism ; Hematopoietic Stem Cells/metabolism ; Humans ; Mutation ; Proteasome Endopeptidase Complex/genetics ; Proteasome Endopeptidase Complex/metabolism ; Protein Binding ; Protein Structure, Tertiary ; Proteolysis ; Suppressor of Cytokine Signaling Proteins/genetics ; Suppressor of Cytokine Signaling Proteins/metabolism ; Ubiquitin/genetics ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination/physiology
Chemical Substances	ASB2 protein, human ; FLNA protein, human ; Filamins ; Suppressor of Cytokine Signaling Proteins ; Ubiquitin ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2013-09-19
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M113.496604
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Article ; Online: Filamins in mechanosensing and signaling.

Razinia, Ziba / Mäkelä, Toni / Ylänne, Jari / Calderwood, David A

Annual review of biophysics

2012 Volume 41, Page(s) 227–246

Abstract: Filamins are essential, evolutionarily conserved, modular, multidomain, actin-binding proteins that organize the actin cytoskeleton and maintain extracellular matrix connections by anchoring actin filaments to transmembrane receptors. By cross-linking ... ...

Abstract	Filamins are essential, evolutionarily conserved, modular, multidomain, actin-binding proteins that organize the actin cytoskeleton and maintain extracellular matrix connections by anchoring actin filaments to transmembrane receptors. By cross-linking and anchoring actin filaments, filamins stabilize the plasma membrane, provide cellular cortical rigidity, and contribute to the mechanical stability of the plasma membrane and the cell cortex. In addition to binding actin, filamins interact with more than 90 other binding partners including intracellular signaling molecules, receptors, ion channels, transcription factors, and cytoskeletal and adhesion proteins. Thus, filamins scaffold a wide range of signaling pathways and are implicated in the regulation of a diverse array of cellular functions including motility, maintenance of cell shape, and differentiation. Here, we review emerging structural and functional evidence that filamins are mechanosensors and/or mechanotransducers playing essential roles in helping cells detect and respond to physical forces in their local environment.
MeSH term(s)	Animals ; Cell Membrane/metabolism ; Cell Movement ; Cell Shape ; Contractile Proteins/chemistry ; Contractile Proteins/metabolism ; Cytoskeleton/metabolism ; Filamins ; Humans ; Mechanotransduction, Cellular ; Microfilament Proteins/chemistry ; Microfilament Proteins/metabolism ; Microfilament Proteins/physiology ; Protein Binding ; Protein Structure, Tertiary ; Signal Transduction
Chemical Substances	Contractile Proteins ; Filamins ; Microfilament Proteins
Language	English
Publishing date	2012-02-23
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2434725-5
ISSN	1936-1238 ; 1936-122X
ISSN (online)	1936-1238
ISSN	1936-122X
DOI	10.1146/annurev-biophys-050511-102252
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Article ; Online: Filamin A controls matrix metalloproteinase activity and regulates cell invasion in human fibrosarcoma cells.

Baldassarre, Massimiliano / Razinia, Ziba / Brahme, Nina N / Buccione, Roberto / Calderwood, David A

Journal of cell science

2012 Volume 125, Issue Pt 16, Page(s) 3858–3869

Abstract: Filamins are an important family of actin-binding proteins that, in addition to bundling actin filaments, link cell surface adhesion proteins, signaling receptors and channels to the actin cytoskeleton, and serve as scaffolds for an array of ... ...

Abstract	Filamins are an important family of actin-binding proteins that, in addition to bundling actin filaments, link cell surface adhesion proteins, signaling receptors and channels to the actin cytoskeleton, and serve as scaffolds for an array of intracellular signaling proteins. Filamins are known to regulate the actin cytoskeleton, act as mechanosensors that modulate tissue responses to matrix density, control cell motility and inhibit activation of integrin adhesion receptors. In this study, we extend the repertoire of filamin activities to include control of extracellular matrix (ECM) degradation. We show that knockdown of filamin increases matrix metalloproteinase (MMP) activity and induces MMP2 activation, enhancing the ability of cells to remodel the ECM and increasing their invasive potential, without significantly altering two-dimensional random cell migration. We further show that within filamin A, the actin-binding domain is necessary, but not sufficient, to suppress the ECM degradation seen in filamin-A-knockdown cells and that dimerization and integrin binding are not required. Filamin mutations are associated with neuronal migration disorders and a range of congenital malformations characterized by skeletal dysplasia and various combinations of cardiac, craniofacial and intestinal anomalies. Furthermore, in breast cancers loss of filamin A has been correlated with increased metastatic potential. Our data suggest that effects on ECM remodeling and cell invasion should be considered when attempting to provide cellular explanations for the physiological and pathological effects of altered filamin expression or filamin mutations.
MeSH term(s)	Actins/metabolism ; Cell Adhesion/physiology ; Cell Line, Tumor ; Cell Movement/physiology ; Contractile Proteins/deficiency ; Contractile Proteins/genetics ; Contractile Proteins/metabolism ; Enzyme Activation ; Extracellular Matrix/metabolism ; Extracellular Matrix/pathology ; Fibrosarcoma/enzymology ; Fibrosarcoma/genetics ; Fibrosarcoma/metabolism ; Fibrosarcoma/pathology ; Filamins ; Gene Knockdown Techniques ; Humans ; Integrins/metabolism ; Matrix Metalloproteinase 14 ; Matrix Metalloproteinase 2/metabolism ; Microfilament Proteins/deficiency ; Microfilament Proteins/genetics ; Microfilament Proteins/metabolism ; Neoplasm Invasiveness ; Phenotype ; Protein Structure, Tertiary
Chemical Substances	Actins ; Contractile Proteins ; Filamins ; Integrins ; Microfilament Proteins ; Matrix Metalloproteinase 2 (EC 3.4.24.24) ; MMP14 protein, human (EC 3.4.24.80) ; Matrix Metalloproteinase 14 (EC 3.4.24.80)
Language	English
Publishing date	2012-05-17
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.104018
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Article ; Online: The E3 ubiquitin ligase specificity subunit ASB2α targets filamins for proteasomal degradation by interacting with the filamin actin-binding domain.

Razinia, Ziba / Baldassarre, Massimiliano / Bouaouina, Mohamed / Lamsoul, Isabelle / Lutz, Pierre G / Calderwood, David A

Journal of cell science

2011 Volume 124, Issue Pt 15, Page(s) 2631–2641

Abstract: Filamins are an important family of actin-binding and crosslinking proteins that mediate remodeling of the actin cytoskeleton and maintain extracellular matrix connections by anchoring transmembrane proteins to actin filaments and linking them to ... ...

Abstract	Filamins are an important family of actin-binding and crosslinking proteins that mediate remodeling of the actin cytoskeleton and maintain extracellular matrix connections by anchoring transmembrane proteins to actin filaments and linking them to intracellular signaling cascades. We recently found that filamins are targeted for proteasomal degradation by the E3 ubiquitin ligase specificity subunit ASBα and that acute degradation of filamins through this ubiquitin-proteasome pathway correlates with cell differentiation. Specifically, in myeloid leukemia cells retinoic-acid-induced expression of ASB2α triggers filamin degradation and recapitulates early events crucial for cell differentiation. ASB2α is thought to link substrates to the ubiquitin transferase machinery; however, the mechanism by which ASB2α interacts with filamin to induce degradation remained unknown. Here, we use cell-based and biochemical assays to show that the subcellular localization of ASB2α to actin-rich structures is dependent on filamin and that the actin-binding domain (ABD) of filamin mediates the interaction with ASB2α. Furthermore, we show that the ABD is necessary and sufficient for ASB2α-mediated filamin degradation. We propose that ASB2α exerts its effect by binding the ABD and mediating its polyubiquitylation, so targeting filamins for degradation. These studies provide the molecular basis for ASB2α-mediated filamin degradation and unravel an important mechanism by which filamin levels can be acutely regulated.
MeSH term(s)	Animals ; CHO Cells ; Cell Line, Tumor ; Cells, Cultured ; Contractile Proteins/genetics ; Contractile Proteins/metabolism ; Cricetinae ; Cricetulus ; Filamins ; Fluorescent Antibody Technique ; HeLa Cells ; Humans ; Immunoblotting ; Mice ; Microfilament Proteins/genetics ; Microfilament Proteins/metabolism ; Proteasome Endopeptidase Complex/metabolism ; Protein Binding ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism
Chemical Substances	Contractile Proteins ; Filamins ; Microfilament Proteins ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2011-07-12
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.084343
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Article ; Online: Filamins regulate cell spreading and initiation of cell migration.

Baldassarre, Massimiliano / Razinia, Ziba / Burande, Clara F / Lamsoul, Isabelle / Lutz, Pierre G / Calderwood, David A

PloS one

2009 Volume 4, Issue 11, Page(s) e7830

Abstract: Mammalian filamins (FLNs) are a family of three large actin-binding proteins. FLNa, the founding member of the family, was implicated in migration by cell biological analyses and the identification of FLNA mutations in the neuronal migration disorder ... ...

Abstract	Mammalian filamins (FLNs) are a family of three large actin-binding proteins. FLNa, the founding member of the family, was implicated in migration by cell biological analyses and the identification of FLNA mutations in the neuronal migration disorder periventricular heterotopia. However, recent knockout studies have questioned the relevance of FLNa to cell migration. Here we have used shRNA-mediated knockdown of FLNa, FLNb or FLNa and FLNb, or, alternatively, acute proteasomal degradation of all three FLNs, to generate FLN-deficient cells and assess their ability to migrate. We report that loss of FLNa or FLNb has little effect on migration but that knockdown of FLNa and FLNb, or proteolysis of all three FLNs, impairs migration. The observed defect is primarily a deficiency in initiation of motility rather than a problem with maintenance of locomotion speed. FLN-deficient cells are also impaired in spreading. Re-expression of full length FLNa, but not re-expression of a mutated FLNa lacking immunoglobulin domains 19 to 21, reverts both the spreading and the inhibition of initiation of migration.Our results establish a role for FLNs in cell migration and spreading and suggest that compensation by other FLNs may mask phenotypes in single knockout or knockdown cells. We propose that interactions between FLNs and transmembrane or signalling proteins, mediated at least in part by immunoglobulin domains 19 to 21 are important for both cell spreading and initiation of migration.
MeSH term(s)	Actins/chemistry ; Animals ; Cell Line, Tumor ; Cell Movement ; Contractile Proteins/metabolism ; Contractile Proteins/physiology ; Filamins ; Humans ; Immunoglobulins/chemistry ; Jurkat Cells ; Microfilament Proteins/metabolism ; Microfilament Proteins/physiology ; Models, Biological ; Mutation ; Phenotype ; Proteasome Endopeptidase Complex/metabolism
Chemical Substances	Actins ; Contractile Proteins ; FLNB protein, human ; Filamins ; Immunoglobulins ; Microfilament Proteins ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2009-11-13
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0007830
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Article ; Online: Structural basis of competition between PINCH1 and PINCH2 for binding to the ankyrin repeat domain of integrin-linked kinase.

Chiswell, Brian P / Stiegler, Amy L / Razinia, Ziba / Nalibotski, Elina / Boggon, Titus J / Calderwood, David A

Journal of structural biology

2009 Volume 170, Issue 1, Page(s) 157–163

Abstract: Formation of a heterotrimeric IPP complex composed of integrin-linked kinase (ILK), the LIM domain protein PINCH, and parvin is important for signaling through integrin adhesion receptors. Mammals possess two PINCH genes that are expressed simultaneously ...

Abstract	Formation of a heterotrimeric IPP complex composed of integrin-linked kinase (ILK), the LIM domain protein PINCH, and parvin is important for signaling through integrin adhesion receptors. Mammals possess two PINCH genes that are expressed simultaneously in many tissues. PINCH1 and PINCH2 have overlapping functions and can compensate for one another in many settings; however, isoform-specific functions have been reported and it is proposed that association with a PINCH1- or PINCH2-containing IPP complex may provide a bifurcation point in integrin signaling promoting different cellular responses. Here we report that the LIM1 domains of PINCH1 and PINCH2 directly compete for the same binding site on the ankyrin repeat domain (ARD) of ILK. We determined the 1.9A crystal structure of the PINCH2 LIM1 domain complexed with the ARD of ILK, and show that disruption of this interface by point mutagenesis reduces binding in vitro and alters localization of PINCH2 in cells. These studies provide further evidence for the role of the PINCH LIM1 domain in association with ILK and highlight direct competition as one mechanism for regulating which PINCH isoform predominates in IPP complexes. Differential regulation of PINCH1 and PINCH2 expression may therefore provide a means for altering cellular integrin signaling pathways.
MeSH term(s)	Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Ankyrin Repeat/genetics ; Binding, Competitive ; Crystallization ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/metabolism ; Gene Expression Regulation/genetics ; LIM Domain Proteins ; Membrane Proteins ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis ; Protein Binding ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/metabolism ; Signal Transduction/genetics
Chemical Substances	Adaptor Proteins, Signal Transducing ; DNA-Binding Proteins ; LIM Domain Proteins ; LIMS1 protein, human ; LIMS2 protein, human ; Membrane Proteins ; integrin-linked kinase (EC 2.7.1.-) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2009-12-04
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1032718-6
ISSN	1095-8657 ; 1047-8477
ISSN (online)	1095-8657
ISSN	1047-8477
DOI	10.1016/j.jsb.2009.12.002
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Article ; Online: A FAK-Cas-Rac-lamellipodin signaling module transduces extracellular matrix stiffness into mechanosensitive cell cycling.

Bae, Yong Ho / Mui, Keeley L / Hsu, Bernadette Y / Liu, Shu-Lin / Cretu, Alexandra / Razinia, Ziba / Xu, Tina / Puré, Ellen / Assoian, Richard K

Science signaling

2014 Volume 7, Issue 330, Page(s) ra57

Abstract: Tissue and extracellular matrix (ECM) stiffness is transduced into intracellular stiffness, signaling, and changes in cellular behavior. Integrins and several of their associated focal adhesion proteins have been implicated in sensing ECM stiffness. We ... ...

Abstract	Tissue and extracellular matrix (ECM) stiffness is transduced into intracellular stiffness, signaling, and changes in cellular behavior. Integrins and several of their associated focal adhesion proteins have been implicated in sensing ECM stiffness. We investigated how an initial sensing event is translated into intracellular stiffness and a biologically interpretable signal. We found that a pathway consisting of focal adhesion kinase (FAK), the adaptor protein p130Cas (Cas), and the guanosine triphosphatase Rac selectively transduced ECM stiffness into stable intracellular stiffness, increased the abundance of the cell cycle protein cyclin D1, and promoted S-phase entry. Rac-dependent intracellular stiffening involved its binding partner lamellipodin, a protein that transmits Rac signals to the cytoskeleton during cell migration. Our findings establish that mechanotransduction by a FAK-Cas-Rac-lamellipodin signaling module converts the external information encoded by ECM stiffness into stable intracellular stiffness and mechanosensitive cell cycling. Thus, lamellipodin is important not only in controlling cellular migration but also for regulating the cell cycle in response to mechanical signals.
MeSH term(s)	Animals ; Carrier Proteins/metabolism ; Cell Cycle ; Crk-Associated Substrate Protein/metabolism ; Focal Adhesion Protein-Tyrosine Kinases/metabolism ; Mechanotransduction, Cellular ; Mice ; Signal Transduction
Chemical Substances	Carrier Proteins ; Crk-Associated Substrate Protein ; Focal Adhesion Protein-Tyrosine Kinases (EC 2.7.10.2)
Language	English
Publishing date	2014-06-17
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2417226-1
ISSN	1937-9145 ; 1945-0877
ISSN (online)	1937-9145
ISSN	1945-0877
DOI	10.1126/scisignal.2004838
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Article ; Online: Exogenous hyalin and sea urchin gastrulation. Part IV: a direct adhesion assay - progress in identifying hyalin's active sites.

Ghazarian, Haike / Coyle-Thompson, Catherine / Dalrymple, William / Hutchins-Carroll, Virginia / Metzenberg, Stan / Razinia, Ziba / Carroll, Edward J / Oppenheimer, Steven B

Zygote (Cambridge, England)

2009 Volume 18, Issue 1, Page(s) 17–26

Abstract: In Strongylocentrotus purpuratus the hyalins are a set of three to four rather large glycoproteins (hereafter referred to as 'hyalin'), which are the major constituents of the hyaline layer, the developing sea urchin embryo's extracellular matrix. Recent ...

Abstract	In Strongylocentrotus purpuratus the hyalins are a set of three to four rather large glycoproteins (hereafter referred to as 'hyalin'), which are the major constituents of the hyaline layer, the developing sea urchin embryo's extracellular matrix. Recent research from our laboratories has shown that hyalin is a cell adhesion molecule involved in sea urchin embryo-specific cellular interactions. Other laboratories have shown it to consist of 2-3% carbohydrate and a cloned, sequenced fragment demonstrated repeat domains (HYR) and non-repeat regions. Interest in this molecule has increased because HYR has been identified in organisms as diverse as bacteria, flies, worms, mice and humans, as well as sea urchins. Our laboratories have shown that hyalin appears to mediate a specific cellular interaction that has interested investigators for over a century, archenteron elongation/attachment to the blastocoel roof. We have shown this finding by localizing hyalin on the two components of the cellular interaction and by showing that hyalin and anti-hyalin antibody block the cellular interaction using a quantitative microplate assay. The microplate assay, however, has limitations because it does not directly assess hyalin's effects on the adhesion of the two components of the interaction. Here we have used an elegant direct assay that avoids the limitations, in which we microdissected the two components of the adhesive interaction and tested their re-adhesion to each other, thereby avoiding possible factors in the whole embryos that could confound or confuse results. Using both assays, we found that mild periodate treatment (6 h to 24 h in sodium acetate buffer with 0.2 M sodium periodate at 4 degrees C in the dark) of hyalin eliminates its ability to block the cellular interaction, suggesting that the carbohydrate component(s) may be involved in hyalin's specific adhesive function. This first step is important in identifying the molecular mechanisms of a well known cellular interaction in the NIH-designated sea urchin embryo model, a system that has led to the discovery of scores of physiological mechanisms, including those involved in human health and disease.
MeSH term(s)	Animals ; Cell Adhesion ; Gastrulation ; Hyalin/chemistry ; Sea Urchins/chemistry ; Sea Urchins/cytology ; Sea Urchins/embryology
Language	English
Publishing date	2009-06-08
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1166294-3
ISSN	1469-8730 ; 0967-1994
ISSN (online)	1469-8730
ISSN	0967-1994
DOI	10.1017/S0967199409005498
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Article ; Online: Filamins regulate cell spreading and initiation of cell migration.

Massimiliano Baldassarre / Ziba Razinia / Clara F Burande / Isabelle Lamsoul / Pierre G Lutz / David A Calderwood

PLoS ONE, Vol 4, Iss 11, p e

2009 Volume 7830

Abstract	Mammalian filamins (FLNs) are a family of three large actin-binding proteins. FLNa, the founding member of the family, was implicated in migration by cell biological analyses and the identification of FLNA mutations in the neuronal migration disorder periventricular heterotopia. However, recent knockout studies have questioned the relevance of FLNa to cell migration. Here we have used shRNA-mediated knockdown of FLNa, FLNb or FLNa and FLNb, or, alternatively, acute proteasomal degradation of all three FLNs, to generate FLN-deficient cells and assess their ability to migrate. We report that loss of FLNa or FLNb has little effect on migration but that knockdown of FLNa and FLNb, or proteolysis of all three FLNs, impairs migration. The observed defect is primarily a deficiency in initiation of motility rather than a problem with maintenance of locomotion speed. FLN-deficient cells are also impaired in spreading. Re-expression of full length FLNa, but not re-expression of a mutated FLNa lacking immunoglobulin domains 19 to 21, reverts both the spreading and the inhibition of initiation of migration.Our results establish a role for FLNs in cell migration and spreading and suggest that compensation by other FLNs may mask phenotypes in single knockout or knockdown cells. We propose that interactions between FLNs and transmembrane or signalling proteins, mediated at least in part by immunoglobulin domains 19 to 21 are important for both cell spreading and initiation of migration.
Keywords	Medicine ; R ; Science ; Q
Subject code	572
Language	English
Publishing date	2009-11-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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