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
2006 ◽  
Vol 45 (3B) ◽  
pp. 2328-2332 ◽  
Author(s):  
Kosaku Kato ◽  
Yukiko Ohmori ◽  
Takeomi Mizutani ◽  
Hisashi Haga ◽  
Kazuyo Ohashi ◽  
...  

2008 ◽  
Vol 283 (41) ◽  
pp. 27973-27981 ◽  
Author(s):  
Akira Nomachi ◽  
Michiru Nishita ◽  
Daisuke Inaba ◽  
Masahiro Enomoto ◽  
Mayumi Hamasaki ◽  
...  

2011 ◽  
Vol 25 (7) ◽  
pp. 1231-1243 ◽  
Author(s):  
Leah Rider ◽  
Maria Diakonova

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.


2012 ◽  
Vol 520 (13) ◽  
pp. 3013-3034 ◽  
Author(s):  
Yoav Noam ◽  
Lise Phan ◽  
Shawn McClelland ◽  
Erik M. Manders ◽  
Markus U. Ehrengruber ◽  
...  

1982 ◽  
Vol 121 (3) ◽  
pp. 553-559 ◽  
Author(s):  
Victor E. KOTELIANSKY ◽  
Marina A. GLUKHOVA ◽  
Vladimir P. SHIRINSKY ◽  
Vladimir N. SMIRNOV ◽  
Tatiana L. BUSHUEVA ◽  
...  

2011 ◽  
Vol 71 ◽  
pp. e234
Author(s):  
Fumio Nakamura ◽  
Tomonobu Hida ◽  
Hidenori Muraoka ◽  
Ken-ichi Ogura ◽  
Yoshio Goshima

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