title: ZFPL1, a novel ring finger protein required for cis-Golgi integrity and efficient ER-to-Golgi transport.
abstract: The Golgi apparatus occupies a central position within the secretory pathway, but the molecular mechanisms responsible for its assembly and organization remain poorly understood. We report here the identification of zinc finger protein-like 1 (ZFPL1) as a novel structural component of the Golgi apparatus. ZFPL1 is a conserved and widely expressed integral membrane protein with two predicted zinc fingers at the N-terminus, the second of which is a likely ring domain. ZFPL1 directly interacts with the cis-Golgi matrix protein GM130. Depletion of ZFPL1 results in the accumulation of cis-Golgi matrix proteins in the intermediate compartment (IC) and the tubulation of cis-Golgi and IC membranes. Loss of ZFPL1 function also impairs cis-Golgi assembly following brefeldin A washout and slows the rate of cargo trafficking into the Golgi apparatus. Effects upon Golgi matrix protein localization and cis-Golgi structure can be rescued by wild-type ZFPL1 but not mutants defective in GM130 binding. Together, these data suggest that ZFPL1 has an important function in maintaining the integrity of the cis-Golgi and that it does so through interactions with GM130.
authors.affiliation: Faculty of Life Sciences, University of Manchester, The Michael Smith Building, Manchester, UK.
authors.forename: Chi-Fang
authors.initials: CF
authors.lastname: Chiu
authors.forename: Yashoda
authors.initials: Y
authors.lastname: Ghanekar
authors.forename: Laura
authors.initials: L
authors.lastname: Frost
authors.forename: Aipo
authors.initials: A
authors.lastname: Diao
authors.forename: Daniel
authors.initials: D
authors.lastname: Morrison
authors.forename: Eddie
authors.initials: E
authors.lastname: McKenzie
authors.forename: Martin
authors.initials: M
authors.lastname: Lowe
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001324:Autoantigens / Q000378:metabolism; D002522:Chlorocebus aethiops; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism*; D019281:Dimerization; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006056:Golgi Apparatus / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D008969:Molecular Sequence Data; D010750:Phosphoproteins / Q000737:chemistry / Q000378:metabolism; D021381:Protein Transport; D054829:RING Finger Domains; D034741:RNA, Small Interfering; D051381:Rats; D014709:Vero Cells
chemical_list: D001324:Autoantigens; D004268:DNA-Binding Proteins; C097741:Golgin subfamily A member 2; D008565:Membrane Proteins; D010750:Phosphoproteins; D034741:RNA, Small Interfering; C114477:ZFPL1 protein, human