Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263049 |
Thr199 |
ETKVHRKtLNPAFNE |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
15350218 |
Endogenous WNK1 and Syt2 coimmunoprecipitate and colocalize on a subset of secretory granules in INS-1 cells. Phosphorylation by WNK1 increases the amount of Ca2+ required for Syt2 binding to phospholipid vesicles; mutation of threonine 202, a WNK1 phosphorylation site, partially prevents this change. These findings suggest that phosphorylation of Syts by WNK1 can regulate Ca2+ sensing and the subsequent Ca2+-dependent interactions mediated by Syt C2 domains. . In contrast, WNK1 phosphorylated Syt2 on T202 and T386 within the C2 domains (Figure 6B). |
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