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A role of GTP‐restricted ARL1 in the dissociation of p230/golgin‐245 from trans ‐Golgi network
Author(s) -
Yu ChiaJung,
Huang LienHung,
Li ChunChun,
Hsu ChiaYi,
Lin YiLing,
Lee FangJen Scott
Publication year - 2010
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.24.1_supplement.lb107
Subject(s) - golgi apparatus , gtp' , dissociation (chemistry) , chemistry , gtpase , microbiology and biotechnology , biology , cell , biochemistry , enzyme
The small GTPase, ARL1, regulates the structure and function of the Golgi complex through mechanisms that have been partly elucidated, which include an ability to regulate the recruitment of two GRIP domain proteins, p230/golgin‐245 and golgin‐97, to the Golgi. However, the regulation of dissociation of golgins from the Golgi remains unknown. Here, we report a novel property of GTP‐restricted ARL1, specifically, the ability to mediate the dissociation of p230/golgin‐245, but not golgin‐97 or GCC185, from the Golgi complex. An in vitro binding assay disclosed higher binding affinity of GTP‐restricted ARL1 to golgin‐97 than to p230/golgin‐245 and GCC185. In addition, ARL1 depletion in cells led to weakened association of golgin‐97 with the TGN, but had a less effect on p230/golgin‐245 and GCC185. We infer that different golgins have distinct targeting and dissociation specificities on the Golgi, which are differentially dependent on GTP‐restricted ARL1.