期刊
JOURNAL OF CELL BIOLOGY
卷 163, 期 2, 页码 339-350出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200307046
关键词
Rab8; AP-1; sorting; polarity; MDCK
类别
资金
- NCI NIH HHS [P01 CA046128, CA46128] Funding Source: Medline
- NIGMS NIH HHS [R01 GM029765, GM29765] Funding Source: Medline
The AP-1B clathrin adaptor complex plays a key role in the recognition and intracellular transport of many membrane proteins destined for the basolateral surface of epithelial cells. However, little is known about other components that act in conjunction with AP-1B. We found that the Rab8 GTPase is one such component. Expression of a constitutively activated GTP hydrolysis mutant selectively inhibited basolateral (but not apical) transport of newly synthesized membrane proteins. Moreover, the effects were limited to AP-1B-dependent basolateral cargo; basolateral transport of proteins containing dileucine targeting motifs that do not interact with AP-1B were targeted normally despite overexpression of mutant Rab8. Similar results were obtained for a dominant-negative allele of the Rho GTPase Cdc42, previously implicated in basolateral transport but now shown to be selective for the AP-1B pathway. Rab8-GFP was localized to membranes in the TGN-recycling endosome, together with AP-1B complexes and the closely related but ubiquitously expressed AP-1A complex. However, expression of active Rab8 caused a selective dissociation of AP-1B complexes, reflecting the specificity of Rab8 for AP-1B-dependent transport.
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