A novel motor, KIF13A, transports mannose-6-phosphate receptor to plasma membrane through direct interaction with AP-1 complex

Terunaga Nakagawa, Mitsutoshi Setou, Dae Hyun Seog, Kouetsu Ogasawara, Naoshi Dohmae, Koji Takio, Nobutaka Hirokawa

Research output: Contribution to journalArticlepeer-review

203 Citations (Scopus)

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 β1-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.

Original languageEnglish
Pages (from-to)569-581
Number of pages13
JournalCell
Volume103
Issue number4
DOIs
Publication statusPublished - 2000
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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