Abstract
Seclp, Vps33p, Vps45p and Slylp constitute a family of proteins implicated in vesicle trafficking at distinct stages of the yeast secretory pathway. Several mammalian homologues of Seclp have been described, including n-secI which has been implicated in the regulation of synaptic vesicle docking at the nerve terminal. We have characterized cDNA clones encoding three additional mammalian homologues belonging to this family: r-vps33a and r-vps33b from rat, which are 30 and 26% identical to yeast Vps33p, respectively, and h-vps45 from human which is 38% identical to yeast Vps45p at the amino acid (aa) level. Phylogenetic analysis of 16 Seclp-related proteins from several species is consistent with the hypothesis that the evolution of this gene family parallels the specialization of vesicle trafficking to distinct intracellular compartments. By Northern analysis, each of these genes is expressed in all tissues examined (brain, spleen, lung, liver, skeletal muscle, kidney, testis). While n-secI binds syntaxin la, 2, and 3, r-vps33a, r-vps33b and h-vps45 do not bind any of the known syntaxins. We propose that the three proteins bind as yet unidentified syntaxin homologues involved in vesicle trafficking between the Golgi apparatus, prelysosomal compartment(s), and the lysosome.
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