scholarly journals Neurabin: A Novel Neural Tissue–specific Actin Filament–binding Protein Involved in Neurite Formation

1997 ◽  
Vol 139 (4) ◽  
pp. 951-961 ◽  
Author(s):  
Hiroyuki Nakanishi ◽  
Hiroshi Obaishi ◽  
Ayako Satoh ◽  
Manabu Wada ◽  
Kenji Mandai ◽  
...  
Keyword(s):  
Rat Brain ◽  
Actin Filament ◽  
Binding Protein ◽  
Neural Tissue ◽  
Terminal Region ◽  
Actin Binding ◽  
Calculated Molecular Mass ◽  
Tissue Specific ◽  
Actin Binding Protein ◽  
Neurite Formation

We purified from rat brain a novel actin filament (F-actin)–binding protein of ∼180 kD (p180), which was specifically expressed in neural tissue. We named p180 neurabin (neural tissue–specific F-actin– binding protein). We moreover cloned the cDNA of neurabin from a rat brain cDNA library and characterized native and recombinant proteins. Neurabin was a protein of 1,095 amino acids with a calculated molecular mass of 122,729. Neurabin had one F-actin–binding domain at the NH2-terminal region, one PSD-95, DlgA, ZO-1–like domain at the middle region, a domain known to interact with transmembrane proteins, and domains predicted to form coiled-coil structures at the COOH-terminal region. Neurabin bound along the sides of F-actin and showed F-actin–cross-linking activity. Immunofluorescence microscopic analysis revealed that neurabin was highly concentrated in the synapse of the developed neurons. Neurabin was also concentrated in the lamellipodia of the growth cone during the development of neurons. Moreover, a study on suppression of endogenous neurabin in primary cultured rat hippocampal neurons by treatment with an antisense oligonucleotide showed that neurabin was involved in the neurite formation. Neurabin is a candidate for key molecules in the synapse formation and function.

scholarly journals Cortactin, an actin binding protein, regulates GLUT4 translocation via actin filament remodeling

2011 ◽  
Vol 76 (11) ◽  
pp. 1262-1269 ◽  
Author(s):  
H. Nazari ◽  
A. Khaleghian ◽  
A. Takahashi ◽  
N. Harada ◽  
N. J. G. Webster ◽  
...  
Keyword(s):  
Actin Filament ◽  
Binding Protein ◽  
Actin Binding ◽  
Glut4 Translocation ◽  
Actin Binding Protein

scholarly journals Homotypic dimerization of the actin-binding protein p57/coronin-1 mediated by a leucine zipper motif in the C-terminal region

2005 ◽  
Vol 387 (2) ◽  
pp. 325-331 ◽  
Author(s):  
Teruaki OKU ◽  
Saotomo ITOH ◽  
Rie ISHII ◽  
Kensuke SUZUKI ◽  
William M. NAUSEEF ◽  
...  
Keyword(s):  
Leucine Zipper ◽  
Fluorescent Protein ◽  
Binding Protein ◽  
Coiled Coil ◽  
Terminal Region ◽  
Full Length ◽  
Actin Binding ◽  
Leucine Zipper Motif ◽  
Actin Binding Protein ◽  
Coiled Coil Domain

The actin-binding protein p57/coronin-1, a member of the coronin protein family, is selectively expressed in immune cells, and has been implicated in leucocyte migration and phagocytosis by virtue of its interaction with F-actin (filamentous actin). We previously identified two sites in the N-terminal region of p57/coronin-1 by which it binds actin, and in the present study we examine the role of the leucine zipper motif located in the C-terminal coiled-coil domain in mediating the homotypic association of p57/coronin-1. Recombinant p57/coronin-1 protein in solution formed a homodimer, as analysed by Superose 12 column chromatography and by sucrose density gradient centrifugation. In vivo, a truncated form consisting of the C-terminal coiled-coil domain co-precipitated with full-length p57/coronin-1 when both were co-expressed in COS-1 cells. A chimaeric construct composed of the C-terminal domain of p57/coronin-1 (which lacks the actin-binding sites) fused with green fluorescent protein co-localized with cortical F-actin-rich regions in COS-1 cells only when full-length p57/coronin-1 was expressed simultaneously in the cells, suggesting that the C-terminal region is required for the homotypic association of p57/coronin-1. Furthermore, p57LZ, a polypeptide consisting of the C-terminal 90 amino acid residues of p57/coronin-1, was sufficient for dimerization. When two leucine residues out of the four that constitute the leucine zipper structure in p57LZ or full-length p57 were replaced with alanine residues, the mutants failed to form homodimers. Taken together, these results demonstrate that p57/coronin-1 forms homodimers, that the association is mediated by the leucine zipper structure in the C-terminal region, and that it plays a role in the cross-linking of F-actin in the cell.

scholarly journals Measuring Molecular Interaction between Actin Filament and Actin Binding Protein Governing Mechanical Properties of Cross-Linked F-Actin Network

2009 ◽  
Vol 96 (3) ◽  
pp. 124a
Author(s):  
Hyungsuk Lee ◽  
Benjamin Pelz ◽  
Jorge M. Ferrer ◽  
Fumihiko Nakamura ◽  
Roger D. Kamm ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Actin Filament ◽  
Molecular Interaction ◽  
Binding Protein ◽  
Actin Binding ◽  
Actin Network ◽  
Actin Binding Protein

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

scholarly journals Nexilin: A Novel Actin Filament-binding Protein Localized at Cell–Matrix Adherens Junction

1998 ◽  
Vol 143 (5) ◽  
pp. 1227-1238 ◽  
Author(s):  
Toshihisa Ohtsuka ◽  
Hiroyuki Nakanishi ◽  
Wataru Ikeda ◽  
Ayako Satoh ◽  
Yumiko Momose ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Rat Brain ◽  
Actin Filament ◽  
Binding Protein ◽  
Adherens Junction ◽  
Actin Binding ◽  
Calculated Molecular Weight ◽  
Cell Matrix ◽  
Focal Contacts ◽  
Cell Cell

We isolated two novel actin filament (F-actin)–binding proteins from rat brain and rat 3Y1 fibroblast. They were splicing variants, and we named brain big one b-nexilin and fibroblast small one s-nexilin. b-Nexilin purified from rat brain was a protein of 656 amino acids (aa) with a calculated molecular weight of 78,392, whereas s-nexilin, encoded by the cDNA isolated from rat 3Y1 cells by the reverse transcriptase-PCR method, was a protein of 606 aa with a calculated molecular weight of 71,942. b-Nexilin had two F-actin– binding domains (ABDs) at the NH2-terminal and middle regions, whereas s-nexilin had one ABD at the middle region because 64 aa residues were deleted and 14 aa residues were inserted in the first NH2-terminal ABD of b-nexilin, and thereby the first ABD lost its activity. b- and s-nexilins bound along the sides of F-actin, but only b-nexilin showed F-actin cross-linking activity. b-Nexilin was mainly expressed in brain and testis, whereas s-nexilin was mainly expressed in testis, spleen, and fibroblasts, such as rat 3Y1 and mouse Swiss 3T3 cells, but neither b- nor s-nexilin was detected in liver, kidney, or cultured epithelial cells. An immunofluorescence microscopic study revealed that s-nexilin was colocalized with vinculin, talin, and paxillin at cell– matrix adherens junction (AJ) and focal contacts, but not at cell–cell AJ, in 3Y1 cells. Overexpressed b- and s-nexilins were localized at focal contacts but not at cell–cell AJ. These results indicate that nexilin is a novel F-actin–binding protein localized at cell–matrix AJ.

An actin-binding protein from Acanthamoeba regulates actin filament polymerization and interactions

Nature ◽  
1980 ◽  
Vol 288 (5790) ◽  
pp. 455-459 ◽  
Author(s):  
Gerhard Isenberg ◽  
Ueli Aebi ◽  
Thomas D. Pollard
Keyword(s):  
Actin Filament ◽  
Binding Protein ◽  
Actin Binding ◽  
Actin Binding Protein
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