Implication of ZW10 in membrane trafficking between the endoplasmic reticulum and Golgi

• DOI: 10.1038/sj.emboj.7600135
• Publication Date: 2004-03-18T13:12:48Z
• Authors: Hidenori Hirose; Kohei Arasaki; Naoshi Dohmae; Koji Takio; Kiyotaka Hatsuzawa; Masami Nagahama; Katsuko Tani; Akitsugu Yamamoto; Masaya Tohyama; Mitsuo Tagaya
• Keywords: 0303 health sciences; Qa-SNARE Proteins; Intracellular Signaling Peptides and Proteins; Dyneins; Golgi Apparatus; Membrane Proteins; Nuclear Proteins; Cell Cycle Proteins; Dynactin Complex; Intracellular Membranes; Endoplasmic Reticulum; Cell Line; Protein Transport; 03 medical and health sciences; Gene Expression Regulation; Two-Hybrid System Techniques; Humans; Carrier Proteins; Interphase; Microtubule-Associated Proteins; Protein Binding

ZW10, a dynamitin-interacting protein associated with kinetochores, is known to participate directly in turning off of the spindle checkpoint. In the present study, we show that ZW10 is located in the endoplasmic reticulum as well as in the cytosol during interphase, and forms a subcomplex with RINT-1 (Rad50-interacting protein) and p31 in a large complex comprising syntaxin 18, an endoplasmic reticulum-localized t-SNARE implicated in membrane trafficking. Like conventional syntaxin-binding proteins, ZW10, RINT-1 and p31 dissociated from syntaxin 18 upon Mg(2+)-ATP treatment in the presence of NSF and alpha-SNAP, whereas the subcomplex was not disassembled. Overexpression, microinjection and knockdown experiments revealed that ZW10 is involved in membrane trafficking between the endoplasmic reticulum and Golgi. The present results disclose an unexpected role for a spindle checkpoint protein, ZW10, during interphase.