Zinc finger protein-like 1 (ZFPL1)

Zinc finger protein-like 1 (ZFPL1) is a conserved and widely expressed integral membrane protein primarily localized to the cis-Golgi, where it acts as a structural component of the Golgi matrix[1][3]. ZFPL1 contains two predicted zinc finger domains at its N-terminus, one of which is likely a ring finger, and a C-terminal transmembrane domain[3]. Its main biological function is to maintain the structural integrity of the cis-Golgi through direct interaction with the cis-Golgi matrix protein GM130; loss of ZFPL1 results in disorganization of the cis-Golgi, accumulation of cis-Golgi matrix proteins in the intermediate compartment, and impaired cargo trafficking into the Golgi apparatus[1][3]. ZFPL1 is phosphorylated during mitosis, suggesting a role in Golgi disassembly and reassembly during cell division[3]. Unlike most zinc finger proteins, which are typically transcription factors involved in gene regulation, ZFPL1 does not appear to function in transcription but instead is a structural protein essential for Golgi organization and secretory pathway function[1][3]. ZFPL1 is expressed in all major tissues and is conserved among metazoans but absent from yeast, indicating its role is specific to higher eukaryotes[3]. There is no current evidence that ZFPL1 is a direct therapeutic target, and its involvement in human disease or interaction with drugs has not been reported.

Other names

D11S750MCG4Zinc finger protein MCG4Zinc-finger protein in MEN1 region