Involvement of rabphilin3 in endocytosis through interaction with rabaptin5

Takeshi Ohya, Takuya Sasaki, Masaki Kato, Yoshimi Takai

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48 Citations (Scopus)


Rabphilin3 and rabaptin5 are downstream target molecules of the Rab3 and -5 subfamily small G proteins that are implicated in exocytosis and endocytosis, respectively. We examined here the physical and functional relationship between the Rab3-rabphilin3 and Rab5-rabaptin5 systems. Rabphilin3 interacted with rabaptin5 at the N-terminal region (amino acids 1- 280), which GTP-Rab3A interacted with. The interaction of rabphilin3 with rabaptin5 was inhibited by guanosine 5'-(3-O-thio)triphosphate-Rab3A. Overexpression of the N-terminal fragment of rabphilin3 (amino acids 1-280) inhibited the receptor-mediated endocytosis of transferrin, and this inhibition was overcome by co-transfection with a dominant active mutant of Rab3A or rabaptin5 in PC12 and HeLa cells. These results suggest that rabphilin3, free of GTP-Rab3A, regulates endocytosis through interaction with rabaptin5 after rabphilin3 complexed with GTP-Rab3A regulates exocytosis.

Original languageEnglish
Pages (from-to)613-617
Number of pages5
JournalJournal of Biological Chemistry
Issue number1
Publication statusPublished - Jan 2 1998
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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