The actin binding protein villin controls accessibility of insulin granules to their docking sites

2018 ◽  
Author(s):  
H Mziaut ◽  
J Dehghany ◽  
M Meyer-Hermann ◽  
M Solimena
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

1992 ◽  
Vol 67 (02) ◽  
pp. 252-257 ◽  
Author(s):  
Anne M Aakhus ◽  
J Michael Wilkinson ◽  
Nils Olav Solum

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.


1990 ◽  
Vol 265 (29) ◽  
pp. 17946-17952 ◽  
Author(s):  
P A Johnston ◽  
F X Yu ◽  
G A Reynolds ◽  
H L Yin ◽  
C R Moomaw ◽  
...  

2018 ◽  
Vol 28 (2) ◽  
pp. 79-98 ◽  
Author(s):  
Michael Schnoor ◽  
Theresia E. Stradal ◽  
Klemens Rottner

Oncogene ◽  
2001 ◽  
Vol 20 (38) ◽  
pp. 5366-5372 ◽  
Author(s):  
Joshua N VanHouten ◽  
Harold L Asch ◽  
Bonnie B Asch

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