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Polycystin‐2 associates with the polycystin‐1 homolog, suREJ3, and localizes to the acrosomal region of sea urchin spermatozoa
Author(s) -
Neill Anna T.,
Moy Gary W.,
Vacquier Victor D.
Publication year - 2004
Publication title -
molecular reproduction and development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.745
H-Index - 105
eISSN - 1098-2795
pISSN - 1040-452X
DOI - 10.1002/mrd.20033
Subject(s) - sea urchin , biology , acrosome reaction , microbiology and biotechnology , acrosome , sperm , transmembrane protein , strongylocentrotus purpuratus , biochemistry , genetics , receptor
Polycystin‐2, the protein mutated in type 2 autosomal dominant polycystic kidney disease, is an integral transmembrane protein with nonselective cation channel activity. Here we report on the sea urchin sperm homolog of polycystin‐2 (suPC2). Like other polycystin‐2 family members, suPC2 is a six‐pass transmembrane protein containing C‐terminal cytoplasmic EF hand and coiled‐coil domains. The protein localizes exclusively to the plasma membrane over the sperm acrosomal vesicle. This localization coincides with the previously reported localization of the sea urchin PC1 homolog, suREJ3. Co‐immunoprecipitation shows that suPC2 and suREJ3 are associated in the membrane. The location of suPC2 sug‐gests that it may function as a cation channel mediating the sperm acrosome reaction. The low cation selectivity of PC2 channels would explain data indicating that Na + and Ca 2+ may enter sea urchin sperm through the same channel during the acrosome reaction. Mol. Reprod. Dev. 67: 472–477, 2004. © 2004 Wiley‐Liss, Inc.