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.