scholarly journals Direct Interaction between the Actin-binding Protein Filamin-A and the Inwardly Rectifying Potassium Channel, Kir2.1

2003 ◽  
Vol 278 (43) ◽  
pp. 41988-41997 ◽  
Author(s):  
Laura J. Sampson ◽  
Mark L. Leyland ◽  
Caroline Dart
Keyword(s):  
Potassium Channel ◽  
Binding Protein ◽  
Direct Interaction ◽  
Actin Binding ◽  
Filamin A ◽  
Actin Binding Protein ◽  
Inwardly Rectifying Potassium Channel ◽  
Inwardly Rectifying

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 Identification of membrane proteins mediating the interaction of human platelets

1980 ◽  
Vol 86 (1) ◽  
pp. 77-86 ◽  
Author(s):  
D Phillips ◽  
L Jennings ◽  
H Edwards
Keyword(s):  
Actin Filaments ◽  
Binding Protein ◽  
Membrane Surface ◽  
Direct Interaction ◽  
Cytoskeletal Proteins ◽  
Actin Binding ◽  
Insoluble Residue ◽  
Membrane Glycoproteins ◽  
Actin Binding Protein ◽  
Activated Platelets

Membrane glycoproteins that mediate platelet-platelet interactions were investigated by identifying those associated with the cytoskeletal structures from aggregated platelets. The cytoskeletal structures from washed platelets, thrombin-activated platelets (platelets incubated with thrombin in the presence of mM EDTA to prevent aggregation) and thrombin- aggregated platelets (platelets activated in the presence of mM Ca(++) were prepared by first treating platelet suspensions with 1 percent Triton X-100 and 5 mM EGTA and then isolating the insoluble residue by centrifugation. The readily identifiable structures in electron micrographs of the residue from washed platelets had the shape and dimensions of actin filaments. Analysis of this residue from washed platelets had the shape and dimensions of actin filaments. Analysis of this residue by SDS gel electrophoresis showed that it consisted primarily of three proteins: actin (mol wt = 43,000), myosin (mol wt = 200,000) and a high molecular weight polypeptide (mol wt = 255,000) which had properties indentical to actin-binding protein (filamin). When platelets are activated with thrombin in the presence of EDTA to prevent aggregation, there was a marked increase in the amount of insoluble precipitate in the subsequent Triton extraction. Transmission electron microscopy showed that this residue not only contained the random array of actin filaments as seen above, but also organized structures from individual platelets which appeared as balls of electron-dense filamentous material approximately 1mum in diameter. SDS polyacrylamide gel analysis of the Triton residue of activated platelets showed that this preparation contained more actin, myosin and actin-binding protein than that from washed platelets plus polypeptides with mol wt of 56,000 and 90,000 and other minor polypeptides. Thus, thrombin activation appeared to increase polymerization of actin in association with other cytoskeletal proteins into structures that are observable after Triton extraction. The cytoskeletal structures from thrombin-aggregated platelets were similar to those from thrombin-activated platelets, except that the structural elements from individual platelets remained aggregated rather than randomly dispersed in the actin filaments. This suggested that the membrane components that mediate the direct interaction of platelets were in Triton residue from aggregated platelets. Only a small percentage of the membrane surface proteins and glycoproteins were found in the cytoskeletal structures from either washed platelets or thrombin-activated platelets. In contrast, the aggregated cytoskeletal structures from thrombin-aggregated platelets contained membrane glycoproteins IIb (26 percent of the total in pre-extracted platelets) and III (14 percent), suggesting that one or both of these glycoproteins participate in the direct interaction of platelets during aggregation.

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.

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

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
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