Yip1 domain family member 4 (YIPF4)

Yip1 domain family member 4 (YIPF4) is a conserved, multi-transmembrane domain protein that predominantly localizes to the Golgi apparatus, especially the cis-Golgi. It is essential for maintaining Golgi architecture by forming a complex with its family member YIPF3; loss or knockdown of YIPF4 results in fragmentation of the Golgi, highlighting its role in sustaining Golgi integrity and membrane trafficking between the endoplasmic reticulum and Golgi compartment. YIPF4 is further notable for being part of a heterodimeric complex (YIPF3-YIPF4) that acts as a receptor for Golgiphagy—selective autophagic degradation of Golgi compartments, mediating binding to mammalian Atg8-family proteins required for this process. Structurally, YIPF4 is predicted to have five transmembrane regions, with an N-terminal domain in the cytosol and a C-terminal domain oriented toward the Golgi lumen. Beyond its housekeeping roles, YIPF4 serves as a binding partner for the E5 oncoprotein from Human Papillomavirus (HPV) via their transmembrane domains. This suggests a possible involvement in the viral life cycle, particularly as its expression is modulated in keratinocytes during differentiation and HPV infection, although YIPF4 depletion does not disrupt key E5 functions. There are no known drugs targeting YIPF4, and it is not an established therapeutic target or biomarker. However, dysfunction of YIPF4 impacts intracellular transport, organelle structure, and may contribute to disease processes associated with Golgi perturbation or viral infection.

Other names

FINGER4NBLA11189MGC11061FinGER4YIPFalpha2protein YIPF4putative protein product of Nbla11189YIP1 family member 4