Sequence analysis, expression, and deletion of a vaccinia virus gene encoding a homolog of profilin, a eukaryotic actin-binding protein.

1991 ◽  
Vol 65 (9) ◽  
pp. 4598-4608 ◽  
Author(s):  
R Blasco ◽  
N B Cole ◽  
B Moss
Keyword(s):  
Sequence Analysis ◽  
Vaccinia Virus ◽  
Binding Protein ◽  
Actin Binding ◽  
Gene Encoding ◽  
Actin Binding Protein ◽  
Virus Gene

scholarly journals nPIST: A Novel Actin Binding Protein of trans-Golgi Network

2018 ◽  
Author(s):  
Swagata Das ◽  
Priyanka Dutta ◽  
Mohit Mazumder ◽  
Soma Seal ◽  
Kheerthana Duraivelan ◽  
...  
Keyword(s):  
Sequence Analysis ◽  
Purkinje Cells ◽  
Binding Protein ◽  
Vesicular Trafficking ◽  
Actin Binding ◽  
Perinuclear Region ◽  
Actin Binding Protein ◽  
Golgi Network

Abstractnpist is the neuronal isoform of PIST, a trans-golgi associated protein involved in major modulation of vesicular trafficking. nPIST interacts with glutamate delta2 receptor (GluRδ2) in Purkinje cells. Our study shows nPIST as a novel actin binding protein. Our structure based sequence analysis shows nPIST contains one WH2-like domain. Further our experimental analysis illustrates that fragment of nPIST consisting of WH2-like domain binds to actin. Moreover it was found that nPIST contains several regions involved in interaction with actin. The binding of nPIST to actin through multiple actin binding regions facilitated actin filament stabilization in vitro. In vivo, nPIST localized actin in perinuclear region as a blotch when ectopically expressed.

Regulation of the gene encoding the p24 actin-binding protein in Dictyostelium discoideum

1992 ◽  
Vol 70 (10-11) ◽  
pp. 1047-1054 ◽  
Author(s):  
Michael T. Greenwood ◽  
Adrian Tsang
Keyword(s):  
Dictyostelium Discoideum ◽  
Early Development ◽  
Binding Protein ◽  
Actin Binding ◽  
Protein Synthesis Inhibitor ◽  
Predicted Amino Acid Sequence ◽  
Cdna Clones ◽  
Mrna Levels ◽  
Gene Encoding ◽  
Actin Binding Protein

We have isolated cDNA clones on the basis of sequence similarity to the gene encoding the cyclic cAMP-binding protein CABP1 of Dictyostelium discoideum. The predicted amino acid sequence of the cloned cDNAs shows that the homology to CABP1 is restricted to a region rich in proline, glycine, glutamine, and tyrosine. Sequence comparison indicates that the cloned cDNAs encode the actin-binding protein p24. We have examined by RNA blot hybridization the expression of the gene encoding p24. For cells developed in suspension, the levels of p24 mRNA increase rapidly during early development, reaching a peak at 3–4 h. Addition of high concentrations of exogenous cAMP during the first 4 h of development produced little or no effect on the accumulation of p24 mRNA. Treatment with cAMP during subsequent stages of development reduced the levels of p24 mRNA. We attempted to determine if the synthesis of new proteins during early development is a requirement for the reduction in p24 mRNA levels by treating the cells with protein synthesis inhibitor. Unexpectedly, the addition of the inhibitor cycloheximide resulted in an increase in the level of p24 mRNA. The roles of cycloheximide and cAMP on the expression of the p24 gene are discussed.Key words: Dictyostelium discoideum, actin-binding protein, gene regulation, cAMP, cycloheximide.

scholarly journals Nemaline Myopathy with Minicores Caused by Mutation of the CFL2 Gene Encoding the Skeletal Muscle Actin–Binding Protein, Cofilin-2

2007 ◽  
Vol 80 (1) ◽  
pp. 162-167 ◽  
Author(s):  
Pankaj B. Agrawal ◽  
Rebecca S. Greenleaf ◽  
Kinga K. Tomczak ◽  
Vilma-Lotta Lehtokari ◽  
Carina Wallgren-Pettersson ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Binding Protein ◽  
Nemaline Myopathy ◽  
Actin Binding ◽  
Muscle Actin ◽  
Gene Encoding ◽  
Actin Binding Protein

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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