Abstract:
:Proteins with dibasic retention motifs are subject to retrograde transport to endoplasmic reticulum (ER) by COPI-coated vesicles. As forward transport requires escape from ER retention, general release mechanisms have been expected. Here, KCNK3 potassium channels are shown to bear two cytoplasmic trafficking motifs: an N-terminal dibasic site that binds beta-COP to hold channels in ER and a C-terminal "release" site that binds the ubiquitous intracellular regulator 14-3-3beta on a nonclassical motif in a phosphorylation-dependent fashion to suppress beta-COP binding and allow forward transport. The strategy appears to be common. The major histocompatibility antigen class II-associated invariant chain Iip35 exhibits dibasic retention, carries a release motif, and shows mutually exclusive binding of beta-COP and 14-3-3beta on adjacent N-terminal sites. Other retained proteins are demonstrated to carry functional 14-3-3beta release motifs.
journal_name
Celljournal_title
Cellauthors
O'Kelly I,Butler MH,Zilberberg N,Goldstein SAdoi
10.1016/s0092-8674(02)01040-1subject
Has Abstractpub_date
2002-11-15 00:00:00pages
577-88issue
4eissn
0092-8674issn
1097-4172pii
S0092867402010401journal_volume
111pub_type
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