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Role of ADP‐ribosylation factor domain protein 1 (ARD1/TRIM23) on lysosome biogenesis and function
Author(s) -
Kang Gi Soo,
Cates Krystal,
Pacheco-Rodriguez Gustavo,
Meza-Carmen Victor,
Daniels Mathew,
Connelly Patricia,
Moss Joel,
Vaughan Martha
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.548.1
Subject(s) - lysosome , microbiology and biotechnology , biogenesis , biology , adp ribosylation factor , endosome , autophagy , internalization , ubiquitin , receptor , golgi apparatus , intracellular , biochemistry , enzyme , apoptosis , gene , endoplasmic reticulum
ADP‐ribosylation factor‐domain protein 1 (ARD1/TRIM23) is a 64‐kDa multi‐functional protein containing an N‐terminal E3 ubiquitin ligase sequence, a C‐terminal GTPase (ADP‐ribosylation factor, ARF) domain, and an internal GTPase‐activating region. ARD1 has been implicated in the regulation of innate immunity, as well as the internalization and degradation of growth factor receptors, but biological functions associated with its intracellular localization in lysosomes and Golgi, remain unknown. Therefore, we compared the lysosomal proteome of livers from ARD1‐null (KO) and control mice. Lysosome‐associated membrane proteins (LAMPs) 1, 2, and 3 were significantly more abundant in the livers of KO mice than those of wild‐type (WT) mice. Levels of LAMP2 in mouse embryonic fibroblasts (MEFs) from ARD1‐KO mice were also higher than those from WT mice. Electron microscopic analysis of mouse liver revealed a larger number of primary and secondary lysosomes in KO than WT mice. In addition, the mean sizes of the primary and secondary lysosomes appeared smaller in KO liver samples than in WT. These findings suggest that ARD1 may have a role in lysosome function and warrant further investigation of ARD1 participation in lysosome biogenesis and/or autophagy.