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A novel Ca2+-binding protein, p22, is required for constitutive membrane traffic.

Authors: Barroso, MR  Bernd, KK  DeWitt, ND  Chang, A  Mills, K  Sztul, ES 
Citation: Barroso MR, etal., J Biol Chem 1996 Apr 26;271(17):10183-7.
Pubmed: (View Article at PubMed) PMID:8626580

We have identified a novel protein, p22, required for "constitutive" exocytic membrane traffic. p22 belongs to the EF-hand superfamily of Ca2+-binding proteins and shows extensive similarity to the regulatory subunit of protein phosphatase 2B, calcineurin B. p22 is a cytosolic N-myristoylated protein that undergoes conformational changes upon binding of Ca2+. Antibodies against a p22 peptide block the targeting/fusion of transcytotic vesicles with the apical plasma membrane, but recombinant wild-type p22 overcomes that inhibition. Nonmyristoylated p22, or p22 incapable of undergoing Ca2+-induced conformational changes, cannot reverse the antibody-mediated inhibition. The data suggest that p22 may act by transducing cellular Ca2+ signals to downstream effectors. p22 is ubiquitously expressed, and we propose that its function is required for membrane trafficking events common to many cells.


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CRRD Object Information
CRRD ID: 724726
Created: 2003-10-20
Species: All species
Last Modified: 2003-10-20
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.