scholarly journals The actin-binding protein Lasp promotes Oskar accumulation at the posterior pole of the Drosophila embryo

Development ◽  
2008 ◽  
Vol 136 (1) ◽  
pp. 95-105 ◽  
Author(s):  
R. Suyama ◽  
A. Jenny ◽  
S. Curado ◽  
W. Pellis-van Berkel ◽  
A. Ephrussi
Keyword(s):  
Binding Protein ◽  
Posterior Pole ◽  
Drosophila Embryo ◽  
Actin Binding ◽  
Actin Binding Protein

scholarly journals Structure of Toxoplasma gondii coronin, an actin‐binding protein that relocalizes to the posterior pole of invasive parasites and contributes to invasion and egress

2014 ◽  
Vol 28 (11) ◽  
pp. 4729-4747 ◽  
Author(s):  
Julien Salamun ◽  
Juha P. Kallio ◽  
Wassim Daher ◽  
Dominique Soldati‐Favre ◽  
Inari Kursula
Keyword(s):  
Toxoplasma Gondii ◽  
Binding Protein ◽  
Posterior Pole ◽  
Actin Binding ◽  
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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