A novel motor, KIF13A, transports mannose-6-phosphate receptor to plasma membrane through direct interaction with AP-1 complex.
Cell
; 103(4): 569-81, 2000 Nov 10.
Article
in En
| MEDLINE
| ID: mdl-11106728
ABSTRACT
Intracellular transport mediated by kinesin superfamily proteins (KIFs) is a highly regulated process. The molecular mechanism of KIFs binding to their respective cargoes remains unclear. We report that KIF13A is a novel plus end-directed microtubule-dependent motor protein and associates with beta 1-adaptin, a subunit of the AP-1 adaptor complex. The cargo vesicles of KIF13A contained AP-1 and mannnose-6-phosphate receptor (M6PR). Overexpression of KIF13A resulted in mislocalization of the AP-1 and the M6PR. Functional blockade of KIF13A reduced cell surface expression of the M6PR. Thus, KIF13A transports M6PR-containing vesicles and targets the M6PR from TGN to the plasma membrane via direct interaction with the AP-1 adaptor complex.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Carrier Proteins
/
Cell Membrane
/
Kinesins
/
Receptor, IGF Type 2
/
Molecular Motor Proteins
/
Membrane Proteins
Limits:
Animals
Language:
En
Journal:
Cell
Year:
2000
Document type:
Article
Affiliation country:
Japan