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

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 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 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.

Clathrin Hub Expression Dissociates the Actin-Binding Protein Hip1R from Coated Pits and Disrupts Their Alignment with the Actin Cytoskeleton

Traffic ◽  
2001 ◽  
Vol 2 (11) ◽  
pp. 851-858 ◽  
Author(s):  
Elizabeth M. Bennett ◽  
Chih-Ying Chen ◽  
Asa E. Y. Engqvist-Goldstein ◽  
David G. Drubin ◽  
Frances M. Brodsky
Keyword(s):  
Actin Cytoskeleton ◽  
Binding Protein ◽  
Actin Binding ◽  
Coated Pits ◽  
Actin Binding Protein

Binding of Human Platelet Glycoprotein lb and Actin to Fragments of Actin-Binding Protein

1992 ◽  
Vol 67 (02) ◽  
pp. 252-257 ◽  
Author(s):  
Anne M Aakhus ◽  
J Michael Wilkinson ◽  
Nils Olav Solum
Keyword(s):  
Actin Filaments ◽  
High Speed ◽  
Binding Protein ◽  
Protein A ◽  
Actin Binding ◽  
Platelet Glycoprotein ◽  
Actin Binding Protein ◽  
Crossed Immunoelectrophoresis ◽  
Triton X ◽  
Calpain Inhibitors

SummaryActin-binding protein (ABP) is degraded into fragments of 190 and 90 kDa by calpain. A monoclonal antibody (MAb TI10) against the 90 kDa fragment of ABP coprecipitated with the glycoprotein lb (GP lb) peak observed on crossed immunoelectrophoresis of Triton X-100 extracts of platelets prepared without calpain inhibitors. MAb PM6/317 against the 190 kDa fragment was not coprecipitated with the GP lb peak under such conditions. The 90 kDa fragment was adsorbed on protein A agarose from extracts that had been preincubated with antibodies to GP lb. This supports the idea that the GP Ib-ABP interaction resides in the 90 kDa region of ABP. GP lb was sedimented with the Triton-insoluble actin filaments in trace amounts only, and only after high speed centrifugation (100,000 × g, 3 h). Both the 190 kDa and the 90 kDa fragments of ABP were sedimented with the Triton-insoluble actin filaments.

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