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Article ; Online: Ablation of palladin in adult heart causes dilated cardiomyopathy associated with intercalated disc abnormalities.

Mastrototaro, Giuseppina / Carullo, Pierluigi / Zhang, Jianlin / Scellini, Beatrice / Piroddi, Nicoletta / Nemska, Simona / Filomena, Maria Carmela / Serio, Simone / Otey, Carol A / Tesi, Chiara / Emrich, Fabian / Linke, Wolfgang A / Poggesi, Corrado / Boncompagni, Simona / Bang, Marie-Louise

eLife

2023 Volume 12

Abstract: Palladin (PALLD) belongs to the PALLD/myopalladin (MYPN)/myotilin family of actin-associated immunoglobulin-containing proteins in the sarcomeric Z-line. PALLD is ubiquitously expressed in several isoforms, and its longest 200 kDa isoform, predominantly ... ...

Abstract	Palladin (PALLD) belongs to the PALLD/myopalladin (MYPN)/myotilin family of actin-associated immunoglobulin-containing proteins in the sarcomeric Z-line. PALLD is ubiquitously expressed in several isoforms, and its longest 200 kDa isoform, predominantly expressed in striated muscle, shows high structural homology to MYPN.
MeSH term(s)	Animals ; Humans ; Mice ; Cardiomyopathies/genetics ; Cardiomyopathy, Dilated ; Cytoskeletal Proteins/genetics ; Cytoskeletal Proteins/metabolism ; Mice, Knockout ; Muscle Proteins/metabolism ; Myocardium/metabolism ; Protein Isoforms/genetics
Chemical Substances	Cytoskeletal Proteins ; Muscle Proteins ; palladin protein, mouse ; Protein Isoforms
Language	English
Publishing date	2023-03-16
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.78629
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Article ; Online: Ablation of palladin in adult heart causes dilated cardiomyopathy associated with intercalated disc abnormalities

Giuseppina Mastrototaro / Pierluigi Carullo / Jianlin Zhang / Beatrice Scellini / Nicoletta Piroddi / Simona Nemska / Maria Carmela Filomena / Simone Serio / Carol A Otey / Chiara Tesi / Fabian Emrich / Wolfgang A Linke / Corrado Poggesi / Simona Boncompagni / Marie-Louise Bang

eLife, Vol

2023 Volume 12

Abstract	Palladin (PALLD) belongs to the PALLD/myopalladin (MYPN)/myotilin family of actin-associated immunoglobulin-containing proteins in the sarcomeric Z-line. PALLD is ubiquitously expressed in several isoforms, and its longest 200 kDa isoform, predominantly expressed in striated muscle, shows high structural homology to MYPN. MYPN gene mutations are associated with human cardiomyopathies, whereas the role of PALLD in the heart has remained unknown, partly due to embryonic lethality of PALLD knockout mice. In a yeast two-hybrid screening, CARP/Ankrd1 and FHOD1 were identified as novel interaction partners of PALLD’s N-terminal region. To study the role of PALLD in the heart, we generated conditional (cPKO) and inducible (cPKOi) cardiomyocyte-specific PALLD knockout mice. While cPKO mice exhibited no pathological phenotype, ablation of PALLD in adult cPKOi mice caused progressive cardiac dilation and systolic dysfunction, associated with reduced cardiomyocyte contractility, intercalated disc abnormalities, and fibrosis, demonstrating that PALLD is essential for normal cardiac function. Double cPKO and MYPN knockout (MKO) mice exhibited a similar phenotype as MKO mice, suggesting that MYPN does not compensate for the loss of PALLD in cPKO mice. Altered transcript levels of MYPN and PALLD isoforms were found in myocardial tissue from human dilated and ischemic cardiomyopathy patients, whereas their protein expression levels were unaltered.
Keywords	heart ; cardiomyopathy ; sarcomere ; intercalated disc ; palladin ; myopalladin ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
Subject code	572
Language	English
Publishing date	2023-03-01T00:00:00Z
Publisher	eLife Sciences Publications Ltd
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: The actin crosslinking protein palladin modulates force generation and mechanosensitivity of tumor associated fibroblasts.

Azatov, Mikheil / Goicoechea, Silvia M / Otey, Carol A / Upadhyaya, Arpita

Scientific reports

2016 Volume 6, Page(s) 28805

Abstract: Cells organize actin filaments into higher-order structures by regulating the composition, distribution and concentration of actin crosslinkers. Palladin is an actin crosslinker found in the lamellar actin network and stress fibers, which are critical ... ...

Abstract	Cells organize actin filaments into higher-order structures by regulating the composition, distribution and concentration of actin crosslinkers. Palladin is an actin crosslinker found in the lamellar actin network and stress fibers, which are critical for mechanosensing of the environment. Palladin also serves as a molecular scaffold for α-actinin, another key actin crosslinker. By virtue of its close interactions with actomyosin structures in the cell, palladin may play an important role in cell mechanics. However, the role of palladin in cellular force generation and mechanosensing has not been studied. Here, we investigate the role of palladin in regulating the plasticity of the actin cytoskeleton and cellular force generation in response to alterations in substrate stiffness. Traction force microscopy revealed that tumor-associated fibroblasts generate larger forces on substrates of increased stiffness. Contrary to expectations, knocking down palladin increased the forces generated by cells and inhibited their ability to sense substrate stiffness for very stiff gels. This was accompanied by significant differences in actin organization, adhesion dynamics and altered myosin organization in palladin knock-down cells. Our results suggest that actin crosslinkers such as palladin and myosin motors coordinate for optimal cell function and to prevent aberrant behavior as in cancer metastasis.
MeSH term(s)	Actins/metabolism ; Cancer-Associated Fibroblasts/drug effects ; Cancer-Associated Fibroblasts/physiology ; Cell Adhesion ; Cells, Cultured ; Cytoskeletal Proteins/physiology ; Focal Adhesions/metabolism ; Heterocyclic Compounds, 4 or More Rings/pharmacology ; Humans ; Mechanotransduction, Cellular ; Phosphoproteins/physiology
Chemical Substances	Actins ; Cytoskeletal Proteins ; Heterocyclic Compounds, 4 or More Rings ; PALLD protein, human ; Phosphoproteins ; blebbistatin (20WC4J7CQ6)
Language	English
Publishing date	2016-06-29
Publishing country	England
Document type	Journal Article ; 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/srep28805
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Article ; Online: Palladin Compensates for the Arp2/3 Complex and Supports Actin Structures during

Dhanda, Aaron S / Vogl, A Wayne / Albraiki, Sharifah E / Otey, Carol A / Beck, Moriah R / Guttman, Julian A

mBio

2018 Volume 9, Issue 2

Abstract: Palladin is an important component of motile actin-rich structures and nucleates branched actin filament ... ...

Abstract	Palladin is an important component of motile actin-rich structures and nucleates branched actin filament arrays
MeSH term(s)	Actin-Related Protein 2-3 Complex/antagonists & inhibitors ; Actin-Related Protein 2-3 Complex/metabolism ; Actins/metabolism ; Animals ; Cell Line ; Cytoskeletal Proteins/metabolism ; Endocytosis ; Host-Pathogen Interactions ; Humans ; Indoles/metabolism ; Listeria monocytogenes/physiology ; Locomotion ; Phosphoproteins/metabolism
Chemical Substances	Actin-Related Protein 2-3 Complex ; Actins ; CK-0944666 ; Cytoskeletal Proteins ; Indoles ; PALLD protein, human ; Phosphoproteins
Language	English
Publishing date	2018-04-10
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2557172-2
ISSN	2150-7511 ; 2161-2129
ISSN (online)	2150-7511
ISSN	2161-2129
DOI	10.1128/mBio.02259-17
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Article ; Online: Actin dynamics regulate subcellular localization of the F-actin-binding protein PALLD in mouse Sertoli cells.

Niedenberger, Bryan A / Chappell, Vesna A / Otey, Carol A / Geyer, Christopher B

Reproduction (Cambridge, England)

2014 Volume 148, Issue 4, Page(s) 333–341

Abstract: Sertoli cells undergo terminal differentiation at puberty to support all phases of germ cell development, which occurs in the mouse beginning in the second week of life. By ∼18 days postpartum (dpp), nearly all Sertoli cells have ceased proliferation. ... ...

Abstract	Sertoli cells undergo terminal differentiation at puberty to support all phases of germ cell development, which occurs in the mouse beginning in the second week of life. By ∼18 days postpartum (dpp), nearly all Sertoli cells have ceased proliferation. This terminal differentiation is accompanied by the development of unique and regionally concentrated filamentous actin (F-actin) structures at the basal and apical aspects of the seminiferous epithelium, and this reorganization is likely to involve the action of actin-binding proteins. Palladin (PALLD) is a widely expressed F-actin-binding and bundling protein recently shown to regulate these structures, yet it is predominantly nuclear in Sertoli cells at puberty. We found that PALLD localized within nuclei of primary Sertoli cells grown in serum-free media but relocalized to the cytoplasm upon serum stimulation. We utilized this system with in vivo relevance to Sertoli cell development to investigate mechanisms regulating nuclear localization of this F-actin-binding protein. Our results indicate that PALLD can be shuttled from the nucleus to the cytoplasm, and that this relocalization occurred following depolymerization of the F-actin cytoskeleton in response to cAMP signaling. Nuclear localization was reduced in Hpg-mutant testes, suggesting the involvement of gonadotropin signaling. We found that PALLD nuclear localization was unaffected in testis tissues from LH receptor and androgen receptor-mutant mice. However, PALLD nuclear localization was reduced in the testes of FSH receptor-mutant mice, suggesting that FSH signaling during Sertoli cell maturation regulates this subcellular localization.
MeSH term(s)	Actin Cytoskeleton/metabolism ; Actins/metabolism ; Active Transport, Cell Nucleus ; Animals ; Cells, Cultured ; Cyclic AMP/metabolism ; Cytoplasm/metabolism ; Cytoskeletal Proteins/metabolism ; Follicle Stimulating Hormone/metabolism ; Gonadotropin-Releasing Hormone/genetics ; Gonadotropin-Releasing Hormone/metabolism ; Humans ; Karyopherins/metabolism ; Luteinizing Hormone/metabolism ; Male ; Mice ; Mice, Knockout ; Phosphoproteins/metabolism ; Protein Precursors/genetics ; Protein Precursors/metabolism ; Receptors, Androgen/genetics ; Receptors, Androgen/metabolism ; Receptors, Cytoplasmic and Nuclear/metabolism ; Receptors, FSH/genetics ; Receptors, FSH/metabolism ; Receptors, LH/genetics ; Receptors, LH/metabolism ; Sertoli Cells/metabolism ; rho GTP-Binding Proteins/metabolism ; Exportin 1 Protein
Chemical Substances	Actins ; Cytoskeletal Proteins ; Karyopherins ; Phosphoproteins ; Protein Precursors ; Receptors, Androgen ; Receptors, Cytoplasmic and Nuclear ; Receptors, FSH ; Receptors, LH ; palladin protein, mouse ; progonadoliberin I ; Gonadotropin-Releasing Hormone (33515-09-2) ; Luteinizing Hormone (9002-67-9) ; Follicle Stimulating Hormone (9002-68-0) ; Cyclic AMP (E0399OZS9N) ; rho GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2014-07-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2034501-X
ISSN	1741-7899 ; 1470-1626 ; 1476-3990
ISSN (online)	1741-7899
ISSN	1470-1626 ; 1476-3990
DOI	10.1530/REP-14-0147
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Article ; Online: Morphology and viscoelasticity of actin networks formed with the mutually interacting crosslinkers: palladin and alpha-actinin.

Grooman, Brian / Fujiwara, Ikuko / Otey, Carol / Upadhyaya, Arpita

PloS one

2012 Volume 7, Issue 8, Page(s) e42773

Abstract: Actin filaments and associated actin binding proteins play an essential role in governing the mechanical properties of eukaryotic cells. Even though cells have multiple actin binding proteins (ABPs) that exist simultaneously to maintain the structural ... ...

Abstract	Actin filaments and associated actin binding proteins play an essential role in governing the mechanical properties of eukaryotic cells. Even though cells have multiple actin binding proteins (ABPs) that exist simultaneously to maintain the structural and mechanical integrity of the cellular cytoskeleton, how these proteins work together to determine the properties of actin networks is not clearly understood. The ABP, palladin, is essential for the maintenance of cell morphology and the regulation of cell movement. Palladin coexists with α-actinin in stress fibers and focal adhesions and binds to both actin and α-actinin. To obtain insight into how mutually interacting actin crosslinking proteins modulate the properties of actin networks, we characterized the micro-structure and mechanics of actin networks crosslinked with palladin and α-actinin. We first showed that palladin crosslinks actin filaments into bundled networks which are viscoelastic in nature. Our studies also showed that composite networks of α-actinin/palladin/actin behave very similar to pure palladin or pure [Formula: see text]-actinin networks. However, we found evidence that palladin and α-actinin synergistically modify network viscoelasticity. To our knowledge, this is the first quantitative characterization of the physical properties of actin networks crosslinked with two mutually interacting crosslinkers.
MeSH term(s)	Actinin/chemistry ; Actins/chemistry ; Biopolymers/chemistry ; Cytoskeletal Proteins/chemistry ; Elasticity ; Phosphoproteins/chemistry ; Protein Binding ; Protein Conformation ; Viscosity
Chemical Substances	Actins ; Biopolymers ; Cytoskeletal Proteins ; PALLD protein, human ; Phosphoproteins ; Actinin (11003-00-2)
Language	English
Publishing date	2012-08-16
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0042773
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Article ; Online: Structural characterization of the interactions between palladin and α-actinin.

Beck, Moriah R / Otey, Carol A / Campbell, Sharon L

Journal of molecular biology

2011 Volume 413, Issue 3, Page(s) 712–725

Abstract: The interaction between α-actinin and palladin, two actin-cross-linking proteins, is essential for proper bidirectional targeting of these proteins. As a first step toward understanding the role of this complex in organizing cytoskeletal actin, we have ... ...

Abstract	The interaction between α-actinin and palladin, two actin-cross-linking proteins, is essential for proper bidirectional targeting of these proteins. As a first step toward understanding the role of this complex in organizing cytoskeletal actin, we have characterized binding interactions between the EF-hand domain of α-actinin (Act-EF34) and peptides derived from palladin and generated an NMR-derived structural model for the Act-EF34/palladin peptide complex. The critical binding site residues are similar to an α-actinin binding motif previously suggested for the complex between Act-EF34 and titin Z-repeats. The structure-based model of the Act-EF34/palladin peptide complex expands our understanding of binding specificity between the scaffold protein α-actinin and various ligands, which appears to require an α-helical motif containing four hydrophobic residues, common to many α-actinin ligands. We also provide evidence that the Family X mutation in palladin, associated with a highly penetrant form of pancreatic cancer, does not interfere with α-actinin binding.
MeSH term(s)	Actinin/chemistry ; Actinin/metabolism ; Binding Sites ; Circular Dichroism ; Crystallography, X-Ray ; Cytoskeletal Proteins/chemistry ; Cytoskeletal Proteins/metabolism ; EF Hand Motifs ; Humans ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Phosphoproteins/chemistry ; Phosphoproteins/metabolism ; Protein Binding ; Protein Conformation
Chemical Substances	ACTN2 protein, human ; Cytoskeletal Proteins ; PALLD protein, human ; Phosphoproteins ; Actinin (11003-00-2)
Language	English
Publishing date	2011-09-08
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2011.08.059
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Article: Identification of palladin isoforms and characterization of an isoform-specific interaction between Lasp-1 and palladin.

Rachlin, Andrew S / Otey, Carol A

Journal of cell science

2006 Volume 119, Issue Pt 6, Page(s) 995–1004

Abstract: Palladin is a recently described phosphoprotein with an important role in cytoskeletal organization. The major palladin isoform (90-92 kDa) binds to three actin-associated proteins (ezrin, VASP and alpha-actinin), suggesting that palladin functions as a ... ...

Abstract	Palladin is a recently described phosphoprotein with an important role in cytoskeletal organization. The major palladin isoform (90-92 kDa) binds to three actin-associated proteins (ezrin, VASP and alpha-actinin), suggesting that palladin functions as a cytoskeletal scaffold. Here, we describe the organization of the palladin gene, which encodes multiple isoforms, including one (140 kDa) with a similar localization pattern to 90 kDa palladin. Overexpression of the 90 kDa or 140 kDa isoforms in COS-7 cells results in rearrangements of the actin cytoskeleton into super-robust bundles and star-like arrays, respectively. Sequence analysis of 140 kDa palladin revealed a conserved binding site for SH3 domains, suggesting that it binds directly to the SH3-domain protein Lasp-1. Binding of 140 kDa palladin, but not 90 kDa palladin, to Lasp-1 was confirmed by yeast two-hybrid and GST-pull-down assays. Isoform-specific siRNA experiments suggested that 140 kDa palladin plays a role in recruiting Lasp-1 to stress fibers. These results add Lasp-1, an actin-binding protein with a crucial role in cell motility, to the growing list of palladin's binding partners, and suggest that 140 kDa palladin has a specialized function in organizing the actin arrays that participate in cell migration and/or cellular contractility.
MeSH term(s)	Actins/metabolism ; Amino Acid Sequence ; Animals ; Binding Sites ; COS Cells ; Cercopithecus aethiops ; Cytoskeletal Proteins/genetics ; Cytoskeletal Proteins/metabolism ; Cytoskeleton/metabolism ; Gene Expression Regulation ; Homeodomain Proteins/genetics ; Homeodomain Proteins/metabolism ; LIM Domain Proteins ; Mice ; Microfilament Proteins/genetics ; Microfilament Proteins/metabolism ; Molecular Sequence Data ; Neoplasm Proteins/genetics ; Neoplasm Proteins/metabolism ; Organ Specificity ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; Protein Binding ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; src Homology Domains
Chemical Substances	Actins ; Cytoskeletal Proteins ; Homeodomain Proteins ; LIM Domain Proteins ; Lasp1 protein, mouse ; Microfilament Proteins ; Neoplasm Proteins ; Phosphoproteins ; Protein Isoforms ; palladin protein, mouse
Language	English
Publishing date	2006-03-15
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.02825
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Article: Alpha-actinin revisited: a fresh look at an old player.

Otey, Carol A / Carpen, Olli

Cell motility and the cytoskeleton

2004 Volume 58, Issue 2, Page(s) 104–111

MeSH term(s)	Actinin/chemistry ; Actinin/metabolism ; Animals ; Cell Adhesion/physiology ; Cell Movement/physiology ; Cytoskeleton/chemistry ; Cytoskeleton/metabolism ; Humans ; Kidney Glomerulus/metabolism ; Protein Structure, Secondary ; Stress Fibers/metabolism ; Synapses/physiology
Chemical Substances	Actinin (11003-00-2)
Language	English
Publishing date	2004-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	283774-2
ISSN	1097-0169 ; 0886-1544
ISSN (online)	1097-0169
ISSN	0886-1544
DOI	10.1002/cm.20007
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Article ; Online: Tumor-Selective Altered Glycosylation and Functional Attenuation of CD73 in Human Hepatocellular Carcinoma.

Alcedo, Karel P / Guerrero, Andres / Basrur, Venkatesha / Fu, Dong / Richardson, Monea L / McLane, Joshua S / Tsou, Chih-Chiang / Nesvizhskii, Alexey I / Welling, Theodore H / Lebrilla, Carlito B / Otey, Carol A / Kim, Hong Jin / Omary, M Bishr / Snider, Natasha T

Hepatology communications

2019 Volume 3, Issue 10, Page(s) 1400–1414

Abstract: CD73, a cell- ... ...

Abstract	CD73, a cell-surface
Language	English
Publishing date	2019-08-09
Publishing country	United States
Document type	Journal Article
ISSN	2471-254X
ISSN (online)	2471-254X
DOI	10.1002/hep4.1410
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