Mutants in trs 120 disrupt traffic from the early endosome to the late Golgi

Huaqing Cai, Yueyi Zhang, Marc Pypaert, Lee Walker, Susan Ferro-Novick

Research output: Contribution to journalArticlepeer-review

93 Scopus citations


Transport protein particle (TRAPP), a large complex that mediates membrane traffic, is found in two forms (TRAPPI and -II). Both complexes share seven subunits, whereas three subunits (Trs130p, -120p, and -65p) are specific to TRAPPII. Previous studies have shown that mutations in the TRAPPII-specific gene trs130 block traffic through or from the Golgi. Surprisingly, we report that mutations in trs120 do not block general secretion. Instead, trs120 mutants accumulate aberrant membrane structures that resemble Berkeley bodies and disrupt the traffic of proteins that recycle through the early endosome. Mutants defective in recycling also display a defect in the localization of coat protein I (COPI) subunits, implying that Trs120p may participate in a COPI-dependent trafficking step on the early endosomal pathway. Furthermore, we demonstrate that Trs120p largely colocalizes with the late Golgi marker Sec7p. Our findings imply that Trs120p is required for vesicle traffic from the early endosome to the late Golgi.

Original languageEnglish (US)
Pages (from-to)823-833
Number of pages11
JournalJournal of Cell Biology
Issue number5
StatePublished - Dec 5 2005
Externally publishedYes

ASJC Scopus subject areas

  • Cell Biology


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