scholarly journals Distinct regional and subcellular localization of the actin-binding protein filamin a in the mature rat brain

2012 ◽  
Vol 520 (13) ◽  
pp. 3013-3034 ◽  
Author(s):  
Yoav Noam ◽  
Lise Phan ◽  
Shawn McClelland ◽  
Erik M. Manders ◽  
Markus U. Ehrengruber ◽  
...  
Keyword(s):  
Subcellular Localization ◽  
Rat Brain ◽  
Binding Protein ◽  
Actin Binding ◽  
Filamin A ◽  
Actin Binding Protein

The Role of Actin-Binding Protein Filamin A in Cellular Stiffness and Morphology Studied by Wide-Range Scanning Probe Microscopy

2006 ◽  
Vol 45 (3B) ◽  
pp. 2328-2332 ◽  
Author(s):  
Kosaku Kato ◽  
Yukiko Ohmori ◽  
Takeomi Mizutani ◽  
Hisashi Haga ◽  
Kazuyo Ohashi ◽  
...  
Keyword(s):  
Scanning Probe Microscopy ◽  
Binding Protein ◽  
Scanning Probe ◽  
Actin Binding ◽  
Filamin A ◽  
Probe Microscopy ◽  
Actin Binding Protein ◽  
Wide Range ◽  
Range Scanning

scholarly journals Receptor Tyrosine Kinase Ror2 Mediates Wnt5a-induced Polarized Cell Migration by Activating c-Jun N-terminal Kinase via Actin-binding Protein Filamin A

2008 ◽  
Vol 283 (41) ◽  
pp. 27973-27981 ◽  
Author(s):  
Akira Nomachi ◽  
Michiru Nishita ◽  
Daisuke Inaba ◽  
Masahiro Enomoto ◽  
Mayumi Hamasaki ◽  
...  
Keyword(s):  
Cell Migration ◽  
Tyrosine Kinase ◽  
Receptor Tyrosine Kinase ◽  
Binding Protein ◽  
Actin Binding ◽  
Filamin A ◽  
Actin Binding Protein

scholarly journals The cytoskeleton actin binding protein filamin A impairs both IGF2 mitogenic effects and the efficacy of IGF1R inhibitors in adrenocortical cancer cells

2021 ◽  
Vol 497 ◽  
pp. 77-88
Author(s):  
R. Catalano ◽  
E. Giardino ◽  
D. Treppiedi ◽  
F. Mangili ◽  
V. Morelli ◽  
...  
Keyword(s):  
Cancer Cells ◽  
Binding Protein ◽  
Actin Binding ◽  
Filamin A ◽  
Adrenocortical Cancer ◽  
Actin Binding Protein

scholarly journals Adapter Protein SH2B1β Binds Filamin A to Regulate Prolactin-Dependent Cytoskeletal Reorganization and Cell Motility

2011 ◽  
Vol 25 (7) ◽  
pp. 1231-1243 ◽  
Author(s):  
Leah Rider ◽  
Maria Diakonova
Keyword(s):  
Actin Cytoskeleton ◽  
Cell Motility ◽  
Binding Protein ◽  
Sh2 Domain ◽  
Actin Binding ◽  
Adapter Protein ◽  
Deficient Mutant ◽  
Filamin A ◽  
Actin Binding Protein ◽  
Dependent Cell

Abstract Prolactin (PRL) regulates cytoskeletal rearrangement and cell motility. PRL-activated Janus tyrosine kinase 2 (JAK2) phosphorylates the p21-activated serine-threonine kinase (PAK)1 and the Src homology 2 (SH2) domain-containing adapter protein SH2B1β. SH2B1β is an actin-binding protein that cross-links actin filaments, whereas PAK1 regulates the actin cytoskeleton by different mechanisms, including direct phosphorylation of the actin-binding protein filamin A (FLNa). Here, we have used a FLNa-deficient human melanoma cell line (M2) and its derivative line (A7) that stably expresses FLNa to demonstrate that SH2B1β and FLNa are required for maximal PRL-dependent cell ruffling. We have found that in addition to two actin-binding domains, SH2B1β has a FLNa-binding domain (amino acids 200–260) that binds directly to repeats 17–23 of FLNa. The SH2B1β-FLNa interaction participates in PRL-dependent actin rearrangement. We also show that phosphorylation of the three tyrosines of PAK1 by JAK2, as well as the presence of FLNa, play a role in PRL-dependent cell ruffling. Finally, we show that the actin- and FLNa-binding-deficient mutant of SH2B1β (SH2B1β 3Δ) abolished PRL-dependent ruffling and PRL-dependent cell migration when expressed along with PAK1 Y3F (JAK2 tyrosyl-phosphorylation-deficient mutant). Together, these data provide insight into a novel mechanism of PRL-stimulated regulation of the actin cytoskeleton and cell motility via JAK2 signaling through FLNa, PAK1, and SH2B1β. We propose a model for PRL-dependent regulation of the actin cytoskeleton that integrates our findings with previous studies.

A Structural Study of Filamin, a Hight-Molecular-Weight Actin-Binding Protein from Chicken Gizzard

1982 ◽  
Vol 121 (3) ◽  
pp. 553-559 ◽  
Author(s):  
Victor E. KOTELIANSKY ◽  
Marina A. GLUKHOVA ◽  
Vladimir P. SHIRINSKY ◽  
Vladimir N. SMIRNOV ◽  
Tatiana L. BUSHUEVA ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Structural Study ◽  
Binding Protein ◽  
Actin Binding ◽  
Filamin A ◽  
Actin Binding Protein ◽  
Chicken Gizzard

scholarly journals Interaction of p38 and Sp1 in a Mechanical Force-induced, β1Integrin-mediated Transcriptional Circuit That Regulates the Actin-binding Protein Filamin-A

2002 ◽  
Vol 277 (49) ◽  
pp. 47541-47550 ◽  
Author(s):  
Mario D'Addario ◽  
Pamela D. Arora ◽  
Richard P. Ellen ◽  
Christopher A. G. McCulloch
Keyword(s):  
Binding Protein ◽  
Mechanical Force ◽  
Actin Binding ◽  
Filamin A ◽  
Actin Binding Protein

scholarly journals Actin dynamics regulate subcellular localization of the F-actin-binding protein PALLD in mouse Sertoli cells

Reproduction ◽  
2014 ◽  
Vol 148 (4) ◽  
pp. 333-341 ◽  
Author(s):  
Bryan A Niedenberger ◽  
Vesna A Chappell ◽  
Carol A Otey ◽  
Christopher B Geyer
Keyword(s):  
Subcellular Localization ◽  
Sertoli Cell ◽  
Nuclear Localization ◽  
Sertoli Cells ◽  
Binding Protein ◽  
Terminal Differentiation ◽  
Mutant Mice ◽  
Actin Binding ◽  
Actin Binding Protein ◽  
Receptor Mutant

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 dayspostpartum(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 within vivorelevance 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 inHpg-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.

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