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Organization of the Rab‐GDI/CHM Superfamily: The Functional Basis for Choroideremia Disease
Author(s) -
Alory Christelle,
Balch William E.
Publication year - 2001
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1034/j.1600-0854.2001.20803.x
Subject(s) - choroideremia , rab , biology , gtpase , endocytic cycle , ras superfamily , microbiology and biotechnology , prenylation , transport protein , guanine nucleotide exchange factor , protein family , genetics , gene , biochemistry , endocytosis , cell , gtp' , enzyme
Choroideremia is an X‐chromosome‐linked disease that leads to the degeneration of the choriocapillaris, the retinal pigment epithelium and the photoreceptor layer in the eye. The gene product defective in choroideremia, CHM, is identical to Rab escort protein 1 (REP1). CHM/REP1 is an essential component of the catalytic geranylgeranyltransferase II complex (GGTrII) that delivers newly synthesized small GTPases belonging to the RAB gene family to the catalytic complex for post‐translational modification. CHM/REP family members are evolutionarily related to members of the guanine nucleotide dissociation inhibitor (GDI) family, proteins involved in the recycling of Rab proteins required for vesicular membrane trafficking through the exocytic and endocytic pathways, forming the GDI/CHM superfamily. Biochemical and structural analyses have now revealed a striking parallel in the organization and function of these two families allowing us to generate a general model for GDI/CHM superfamily function in health and disease.