LIVIVO - Search results -

Search results

Result 1 - 8 of total 8

Search options

Article: Publisher Correction: A mechano-signalling network linking microtubules, myosin IIA filaments and integrin-based adhesions.

Rafiq, Nisha Bte Mohd / Nishimura, Yukako / Plotnikov, Sergey V / Thiagarajan, Visalatchi / Zhang, Zhen / Shi, Shidong / Natarajan, Meenubharathi / Viasnoff, Virgile / Kanchanawong, Pakorn / Jones, Gareth E / Bershadsky, Alexander D

Nature materials

2019 Volume 18, Issue 7, Page(s) 770

Abstract: An amendment to this paper has been published and can be accessed via a link at the top of the paper. ...

Abstract	An amendment to this paper has been published and can be accessed via a link at the top of the paper.
Language	English
Publishing date	2019-10-09
Publishing country	England
Document type	Published Erratum
ZDB-ID	2088679-2
ISSN	1476-4660 ; 1476-1122
ISSN (online)	1476-4660
ISSN	1476-1122
DOI	10.1038/s41563-019-0414-4
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Article ; Online: Forces and constraints controlling podosome assembly and disassembly.

Rafiq, Nisha Bte Mohd / Grenci, Gianluca / Lim, Cheng Kai / Kozlov, Michael M / Jones, Gareth E / Viasnoff, Virgile / Bershadsky, Alexander D

Philosophical transactions of the Royal Society of London. Series B, Biological sciences

2019 Volume 374, Issue 1779, Page(s) 20180228

Abstract: Podosomes are a singular category of integrin-mediated adhesions important in the processes of cell migration, matrix degradation and cancer cell invasion. Despite a wealth of biochemical studies, the effects of mechanical forces on podosome integrity ... ...

Abstract	Podosomes are a singular category of integrin-mediated adhesions important in the processes of cell migration, matrix degradation and cancer cell invasion. Despite a wealth of biochemical studies, the effects of mechanical forces on podosome integrity and dynamics are poorly understood. Here, we show that podosomes are highly sensitive to two groups of physical factors. First, we describe the process of podosome disassembly induced by activation of myosin-IIA filament assembly. Next, we find that podosome integrity and dynamics depends upon membrane tension and can be experimentally perturbed by osmotic swelling and deoxycholate treatment. We have also found that podosomes can be disrupted in a reversible manner by single or cyclic radial stretching of the substratum. We show that disruption of podosomes induced by osmotic swelling is independent of myosin-II filaments. The inhibition of the membrane sculpting protein, dynamin-II, but not clathrin, resulted in activation of myosin-IIA filament formation and disruption of podosomes. The effect of dynamin-II inhibition on podosomes was, however, independent of myosin-II filaments. Moreover, formation of organized arrays of podosomes in response to microtopographic cues (the ridges with triangular profile) was not accompanied by reorganization of myosin-II filaments. Thus, mechanical elements such as myosin-II filaments and factors affecting membrane tension/sculpting independently modulate podosome formation and dynamics, underlying a versatile response of these adhesion structures to intracellular and extracellular cues. This article is part of a discussion meeting issue 'Forces in cancer: interdisciplinary approaches in tumour mechanobiology'.
MeSH term(s)	Cell Movement ; Humans ; Nonmuscle Myosin Type IIA/metabolism ; Podosomes/metabolism ; Tumor Cells, Cultured/metabolism
Chemical Substances	Nonmuscle Myosin Type IIA (EC 3.6.1.-)
Language	English
Publishing date	2019-07-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	208382-6
ISSN	1471-2970 ; 0080-4622 ; 0264-3839 ; 0962-8436
ISSN (online)	1471-2970
ISSN	0080-4622 ; 0264-3839 ; 0962-8436
DOI	10.1098/rstb.2018.0228
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Einzelsignatur: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: A mechano-signalling network linking microtubules, myosin IIA filaments and integrin-based adhesions.

Nature materials

2019 Volume 18, Issue 6, Page(s) 638–649

Abstract: The interrelationship between microtubules and the actin cytoskeleton in mechanoregulation of integrin-mediated adhesions is poorly understood. Here, we show that the effects of microtubules on two major types of cell-matrix adhesion, focal adhesions and ...

Abstract	The interrelationship between microtubules and the actin cytoskeleton in mechanoregulation of integrin-mediated adhesions is poorly understood. Here, we show that the effects of microtubules on two major types of cell-matrix adhesion, focal adhesions and podosomes, are mediated by KANK family proteins connecting the adhesion protein talin with microtubule tips. Both total microtubule disruption and microtubule uncoupling from adhesions by manipulations with KANKs trigger a massive assembly of myosin IIA filaments, augmenting focal adhesions and disrupting podosomes. Myosin IIA filaments are indispensable effectors in the microtubule-driven regulation of integrin-mediated adhesions. Myosin IIA filament assembly depends on Rho activation by the RhoGEF GEF-H1, which is trapped by microtubules when they are connected with integrin-mediated adhesions via KANK proteins but released after their disconnection. Thus, microtubule capture by integrin-mediated adhesions modulates the GEF-H1-dependent effect of microtubules on the assembly of myosin IIA filaments. Subsequent actomyosin reorganization then remodels the focal adhesions and podosomes, closing the regulatory loop.
MeSH term(s)	Adaptor Proteins, Signal Transducing ; Apoptosis Regulatory Proteins ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cell Line, Tumor ; Cytoskeletal Proteins ; Focal Adhesions/metabolism ; Humans ; Integrins/metabolism ; Mechanotransduction, Cellular ; Microtubules/metabolism ; Nonmuscle Myosin Type IIA/metabolism ; Podosomes/metabolism ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Rho Guanine Nucleotide Exchange Factors/metabolism ; Tumor Suppressor Proteins/genetics ; Tumor Suppressor Proteins/metabolism ; rho GTP-Binding Proteins/metabolism ; rho-Associated Kinases/metabolism
Chemical Substances	ARHGEF2 protein, human ; Adaptor Proteins, Signal Transducing ; Apoptosis Regulatory Proteins ; Carrier Proteins ; Cytoskeletal Proteins ; Integrins ; KANK1 protein, human ; Kank2 protein, human ; Recombinant Proteins ; Rho Guanine Nucleotide Exchange Factors ; Tumor Suppressor Proteins ; rho-Associated Kinases (EC 2.7.11.1) ; Nonmuscle Myosin Type IIA (EC 3.6.1.-) ; rho GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2019-05-21
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2088679-2
ISSN	1476-4660 ; 1476-1122
ISSN (online)	1476-4660
ISSN	1476-1122
DOI	10.1038/s41563-019-0371-y
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Podosome assembly is controlled by the GTPase ARF1 and its nucleotide exchange factor ARNO.

Rafiq, Nisha Bte Mohd / Lieu, Zi Zhao / Jiang, Tingting / Yu, Cheng-Han / Matsudaira, Paul / Jones, Gareth E / Bershadsky, Alexander D

The Journal of cell biology

2016 Volume 216, Issue 1, Page(s) 181–197

Abstract: Podosomes represent a class of integrin-mediated cell-matrix adhesions formed by migrating and matrix-degrading cells. We demonstrate that in macrophage-like THP1 cells and fibroblasts stimulated to produce podosomes, down-regulation of the G-protein ... ...

Abstract	Podosomes represent a class of integrin-mediated cell-matrix adhesions formed by migrating and matrix-degrading cells. We demonstrate that in macrophage-like THP1 cells and fibroblasts stimulated to produce podosomes, down-regulation of the G-protein ARF1 or the ARF1 guanine nucleotide exchange factor, ARNO, by small, interfering RNA or pharmacological inhibitors led to striking podosome elimination. Concomitantly, treatments inducing podosome formation increased the level of guanosine triphosphate (GTP)-bound ARF1. ARNO was found to colocalize with the adhesive rings of podosomes, whereas ARF1 was localized to vesicular structures transiently contacting podosome rings. Inhibition of ARF1 led to an increase in RhoA-GTP levels and triggered assembly of myosin-IIA filaments in THP1 cells, whereas the suppression of myosin-IIA rescued podosome formation regardless of ARF1 inhibition. Finally, expression of constitutively active ARF1 in fibroblasts induced formation of putative podosome precursors: actin-rich puncta coinciding with matrix degradation sites and containing proteins of the podosome core but not of the adhesive ring. Thus, ARNO-ARF1 regulates formation of podosomes by inhibition of RhoA/myosin-II and promotion of actin core assembly.
MeSH term(s)	ADP-Ribosylation Factor 1/antagonists & inhibitors ; ADP-Ribosylation Factor 1/genetics ; ADP-Ribosylation Factor 1/metabolism ; Actin Cytoskeleton/enzymology ; Actins/metabolism ; Animals ; Cell Line, Tumor ; Enzyme Inhibitors/pharmacology ; GTPase-Activating Proteins/genetics ; GTPase-Activating Proteins/metabolism ; Guanosine Triphosphate/metabolism ; Humans ; Mice ; Microscopy, Fluorescence ; Nonmuscle Myosin Type IIA/metabolism ; Podosomes/drug effects ; Podosomes/enzymology ; RNA Interference ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Time Factors ; Transfection ; rho-Associated Kinases/metabolism ; rhoA GTP-Binding Protein/metabolism
Chemical Substances	Actins ; Enzyme Inhibitors ; GTPase-Activating Proteins ; Recombinant Fusion Proteins ; cytohesin-2 ; RHOA protein, human (124671-05-2) ; Guanosine Triphosphate (86-01-1) ; rho-Associated Kinases (EC 2.7.11.1) ; Nonmuscle Myosin Type IIA (EC 3.6.1.-) ; ADP-Ribosylation Factor 1 (EC 3.6.5.2) ; rhoA GTP-Binding Protein (EC 3.6.5.2)
Language	English
Publishing date	2016-12-22
Publishing country	United States
Document type	Journal Article ; Video-Audio Media
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.201605104
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Ub I Zs.190: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Integrin-matrix clusters form podosome-like adhesions in the absence of traction forces.

Yu, Cheng-han / Rafiq, Nisha Bte Mohd / Krishnasamy, Anitha / Hartman, Kevin L / Jones, Gareth E / Bershadsky, Alexander D / Sheetz, Michael P

Cell reports

2013 Volume 5, Issue 5, Page(s) 1456–1468

Abstract: Matrix-activated integrins can form different adhesion structures. We report that nontransformed fibroblasts develop podosome-like adhesions when spread on fluid Arg-Gly-Asp peptide (RGD)-lipid surfaces, whereas they habitually form focal adhesions on ... ...

Abstract	Matrix-activated integrins can form different adhesion structures. We report that nontransformed fibroblasts develop podosome-like adhesions when spread on fluid Arg-Gly-Asp peptide (RGD)-lipid surfaces, whereas they habitually form focal adhesions on rigid RGD glass surfaces. Similar to classic macrophage podosomes, the podosome-like adhesions are protrusive and characterized by doughnut-shaped RGD rings that surround characteristic core components including F-actin, N-WASP, and Arp2/Arp3. Furthermore, there are 18 podosome markers in these adhesions, though they lack matrix metalloproteinases that characterize invadopodia and podosomes of Src-transformed cells. When nontransformed cells develop force on integrin-RGD clusters by pulling RGD lipids to prefabricated rigid barriers (metal lines spaced by 1-2 μm), these podosomes fail to form and instead form focal adhesions. The formation of podosomes on fluid surfaces is mediated by local activation of phosphoinositide 3-kinase (PI3K) and the production of phosphatidylinositol-(3,4,5)-triphosphate (PIP3) in a FAK/PYK2-dependent manner. Enrichment of PIP3 precedes N-WASP activation and the recruitment of RhoA-GAP ARAP3. We propose that adhesion structures can be modulated by traction force development and that production of PIP3 stimulates podosome formation and subsequent RhoA downregulation in the absence of traction force.
MeSH term(s)	Actin-Related Protein 2-3 Complex/metabolism ; Actins/metabolism ; Animals ; Cell Adhesion ; Cell Line, Tumor ; Extracellular Matrix/metabolism ; Fibroblasts/drug effects ; Fibroblasts/metabolism ; Fibroblasts/physiology ; Focal Adhesion Kinase 1/metabolism ; Focal Adhesion Kinase 2/metabolism ; Focal Adhesions/drug effects ; Focal Adhesions/metabolism ; GTPase-Activating Proteins/metabolism ; Humans ; Integrins/metabolism ; Matrix Metalloproteinases/metabolism ; Oligopeptides/pharmacology ; Phosphatidylinositol 3-Kinases/metabolism ; Phosphatidylinositol Phosphates/metabolism ; Pseudopodia/drug effects ; Pseudopodia/metabolism ; Rats ; Wiskott-Aldrich Syndrome Protein, Neuronal/metabolism
Chemical Substances	Actin-Related Protein 2-3 Complex ; Actins ; GTPase-Activating Proteins ; Integrins ; Oligopeptides ; Phosphatidylinositol Phosphates ; Wasl protein, rat ; Wiskott-Aldrich Syndrome Protein, Neuronal ; phosphatidylinositol 3,4,5-triphosphate ; arginyl-glycyl-aspartic acid (78VO7F77PN) ; Focal Adhesion Kinase 1 (EC 2.7.10.2) ; Focal Adhesion Kinase 2 (EC 2.7.10.2) ; Matrix Metalloproteinases (EC 3.4.24.-)
Language	English
Publishing date	2013-11-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2013.10.040
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Integrin-beta3 clusters recruit clathrin-mediated endocytic machinery in the absence of traction force.

Yu, Cheng-han / Rafiq, Nisha Bte Mohd / Cao, Fakun / Zhou, Yuhuan / Krishnasamy, Anitha / Biswas, Kabir Hassan / Ravasio, Andrea / Chen, Zhongwen / Wang, Yu-Hsiu / Kawauchi, Keiko / Jones, Gareth E / Sheetz, Michael P

Nature communications

2015 Volume 6, Page(s) 8672

Abstract: The turnover of integrin receptors is critical for cell migration and adhesion dynamics. Here we find that force development at integrins regulates adaptor protein recruitment and endocytosis. Using mobile RGD (Arg-Gly-Asp) ligands on supported lipid ... ...

Abstract	The turnover of integrin receptors is critical for cell migration and adhesion dynamics. Here we find that force development at integrins regulates adaptor protein recruitment and endocytosis. Using mobile RGD (Arg-Gly-Asp) ligands on supported lipid membranes (RGD membranes) and rigid RGD ligands on glass (RGD-glass), we find that matrix force-dependent integrin signals block endocytosis. Dab2, an adaptor protein of clathrin-mediated endocytosis, is not recruited to activated integrin-beta3 clusters on RGD-glass; however, it is recruited to integrin-mediated adhesions on RGD membranes. Further, when force generation is inhibited on RGD-glass, Dab2 binds to integrin-beta3 clusters. Dab2 binding to integrin-beta3 excludes other adhesion-related adaptor proteins, such as talin. The clathrin-mediated endocytic machinery combines with Dab2 to facilitate the endocytosis of RGD-integrin-beta3 clusters. From these observations, we propose that loss of traction force on ligand-bound integrin-beta3 causes recruitment of Dab2/clathrin, resulting in endocytosis of integrins.
MeSH term(s)	Adaptor Proteins, Vesicular Transport/genetics ; Adaptor Proteins, Vesicular Transport/metabolism ; Animals ; Biomechanical Phenomena ; Cell Movement ; Cells/chemistry ; Cells/cytology ; Cells/metabolism ; Clathrin/genetics ; Clathrin/metabolism ; Endocytosis ; HeLa Cells ; Humans ; Integrin beta3/genetics ; Integrin beta3/metabolism ; Mice ; Protein Binding ; Traction
Chemical Substances	Adaptor Proteins, Vesicular Transport ; Clathrin ; Dab2 protein, mouse ; Integrin beta3
Language	English
Publishing date	2015-10-28
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2041-1723
ISSN (online)	2041-1723
DOI	10.1038/ncomms9672
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Full text

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- Full text online
- Order with fees

Article ; Online: Integrin-Matrix Clusters Form Podosome-like Adhesions in the Absence of Traction Forces

Cheng-han Yu / Nisha Bte Mohd Rafiq / Anitha Krishnasamy / Kevin L. Hartman / Gareth E. Jones / Alexander D. Bershadsky / Michael P. Sheetz

Cell Reports, Vol 5, Iss 5, Pp 1456-

2013 Volume 1468

Abstract	Matrix-activated integrins can form different adhesion structures. We report that nontransformed fibroblasts develop podosome-like adhesions when spread on fluid Arg-Gly-Asp peptide (RGD)-lipid surfaces, whereas they habitually form focal adhesions on rigid RGD glass surfaces. Similar to classic macrophage podosomes, the podosome-like adhesions are protrusive and characterized by doughnut-shaped RGD rings that surround characteristic core components including F-actin, N-WASP, and Arp2/Arp3. Furthermore, there are 18 podosome markers in these adhesions, though they lack matrix metalloproteinases that characterize invadopodia and podosomes of Src-transformed cells. When nontransformed cells develop force on integrin-RGD clusters by pulling RGD lipids to prefabricated rigid barriers (metal lines spaced by 1–2 μm), these podosomes fail to form and instead form focal adhesions. The formation of podosomes on fluid surfaces is mediated by local activation of phosphoinositide 3-kinase (PI3K) and the production of phosphatidylinositol-(3,4,5)-triphosphate (PIP3) in a FAK/PYK2-dependent manner. Enrichment of PIP3 precedes N-WASP activation and the recruitment of RhoA-GAP ARAP3. We propose that adhesion structures can be modulated by traction force development and that production of PIP3 stimulates podosome formation and subsequent RhoA downregulation in the absence of traction force.
Keywords	Biology (General) ; QH301-705.5
Language	English
Publishing date	2013-12-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

Full text online

Full text

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Branched disulfide-based polyamidoamines capable of mediating high gene transfection.

Khan, Majad / Wiradharma, Nikken / Beniah, Goliath / Rafiq, Nisha Bte Mohd / Liu, Shaoqiong / Au, Juliana / Yang, Yi-Yan

Current pharmaceutical design

2009 Volume 16, Issue 21, Page(s) 2341–2349

Abstract: DNA condensation, endosomal escape of DNA/polymeric complexes, and unpacking of DNA are the key steps in the process of non-viral gene delivery. Amongst these steps, currently the unpacking of the DNA cargo from the DNA/polymeric nanocomplexes is the ... ...

Abstract	DNA condensation, endosomal escape of DNA/polymeric complexes, and unpacking of DNA are the key steps in the process of non-viral gene delivery. Amongst these steps, currently the unpacking of the DNA cargo from the DNA/polymeric nanocomplexes is the most challenging and arguably the most crucial if one wants to achieve high gene transfection with minimum cytotoxicity in the target cell. In this report we review current and past examples in the literature that demonstrate concerted efforts in designing and synthesizing various forms of cationic polymeric vectors having "built in" features. Such features can be certain types of chemical functional groups, such as amines and acids or other degradable bonds like esters, carbonates and disulfides, which allow for breakdown of polymeric vectors in certain cellular compartments. This may lead the DNA cargo to dissociate from the DNA/polymer complexes so as to maximize intracellular gene delivery. Furthermore, we provide further evidence that it is possible to achieve the goal of high gene transfection coupled with low cytotoxicity via rational design and formulation of branched polyamidoamines containing disulfide bonds. The DNA binding ability of these polymers and particle size as well as zeta potential of their DNA complexes were investigated. The cytotoxicity of pure polymer and polymer/DNA complexes at various polymer concentrations was studied in HEK293 human embryonic kidney, HepG2 human liver carcinoma, 4T1 mouse breast cancer and HeLa human cervical cancer cell lines. In vitro gene transfection efficiency induced by polymer/DNA complexes was explored in these cell lines by using luciferase and GFP reporter genes in comparison with PEI.
MeSH term(s)	Animals ; Cell Line ; DNA, Neoplasm/genetics ; DNA, Neoplasm/metabolism ; Disulfides/administration & dosage ; Disulfides/chemical synthesis ; Disulfides/pharmacology ; Gene Transfer Techniques ; HeLa Cells ; Hep G2 Cells ; Humans ; Mice ; Polyamines/administration & dosage ; Polyamines/chemical synthesis ; Polyamines/pharmacology ; Transfection/methods
Chemical Substances	DNA, Neoplasm ; Disulfides ; Poly(amidoamine) ; Polyamines
Language	English
Publishing date	2009-10-20
Publishing country	United Arab Emirates
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1304236-1
ISSN	1873-4286 ; 1381-6128
ISSN (online)	1873-4286
ISSN	1381-6128
DOI	10.2174/138161210791920504
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 4714: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

To top

Your last searches

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

Full text online

More links

Kategorien

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito