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Recruitment of protein kinase D to the trans ‐Golgi network via the first cysteine‐rich domain
Author(s) -
Maeda Yusuke,
Beznoussenko Galina V.,
Lint Johan Van,
Mironov Alexander A.,
Malhotra Vivek
Publication year - 2001
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/20.21.5982
Subject(s) - biology , golgi apparatus , microbiology and biotechnology , cysteine , immunoprecipitation , kinase , serine , cytosol , phosphorylation , fusion protein , protein kinase a , biochemistry , gene , recombinant dna , endoplasmic reticulum , enzyme
Protein kinase D (PKD) is a cytosolic protein, which upon binding to the trans ‐Golgi network (TGN) regulates the fission of transport carriers specifically destined to the cell surface. We have found that the first cysteine‐rich domain (C1a), but not the second cysteine‐rich domain (C1b), is sufficient for the binding of PKD to the TGN. Proline 155 in C1a is necessary for the recruitment of intact PKD to the TGN. Whereas C1a is sufficient to target a reporter protein to the TGN, mutation of serines 744/748 to alanines in the activation loop of intact PKD inhibits its localization to the TGN. Moreover, anti‐phospho‐PKD antibody, which recognizes only the activated form of PKD, recognizes the TGN‐bound PKD. Thus, activation of intact PKD is important for binding to the TGN.