ZFPL1, a novel ring finger protein required for cis-Golgi integrity and efficient ER-to-Golgi transport |
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Authors: | Chiu Chi-Fang Ghanekar Yashoda Frost Laura Diao Aipo Morrison Daniel McKenzie Eddie Lowe Martin |
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Affiliation: | Faculty of Life Sciences, University of Manchester, The Michael Smith Building, Manchester, UK. |
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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. |
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Keywords: | GM130 Golgi apparatus Golgi matrix intermediate compartment ZFPL1 |
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