Phosphatidylinositol 4,5-bisphosphate directs spermatid cell polarity and exocyst localization in Drosophila.

Phosphatidylinositol 4,5-bisphosphate directs spermatid cell polarity and exocyst localization in Drosophila.
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DOI:
10.1091/mbc.e09-07-0582
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发表时间:
2010-05-01
影响因子:
3.3
通讯作者:
Brill JA
Brill JA
中科院分区:
生物学3区
文献类型:
--
作者:
Fabian L;Wei HC;Rollins J;Noguchi T;Blankenship JT;Bellamkonda K;Polevoy G;Gervais L;Guichet A;Fuller MT;Brill JA

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This study identifies phosphoinositides as key regulators of spermatid cell polarity. Polarization and elongation of spermatids in Drosophila are regulated through local synthesis of PIP2 by Sktl, which drives polarized localization of the exocyst complex to promote targeted membrane delivery and polarization of the elongating spermatid cysts. During spermiogenesis, Drosophila melanogaster spermatids coordinate their elongation in interconnected cysts that become highly polarized, with nuclei localizing to one end and sperm tail growth occurring at the other. Remarkably little is known about the signals that drive spermatid polarity and elongation. Here we identify phosphoinositides as critical regulators of these processes. Reduction of plasma membrane phosphatidylinositol 4,5-bisphosphate (PIP2) by low-level expression of the PIP2 phosphatase SigD or mutation of the PIP2 biosynthetic enzyme Skittles (Sktl) results in dramatic defects in spermatid cysts, which become bipolar and fail to fully elongate. Defects in polarity are evident from the earliest stages of elongation, indicating that phosphoinositides are required for establishment of polarity. Sktl and PIP2 localize to the growing end of the cysts together with the exocyst complex. Strikingly, the exocyst becomes completely delocalized when PIP2 levels are reduced, and overexpression of Sktl restores exocyst localization and spermatid cyst polarity. Moreover, the exocyst is required for polarity, as partial loss of function of the exocyst subunit Sec8 results in bipolar cysts. Our data are consistent with a mechanism in which localized synthesis of PIP2 recruits the exocyst to promote targeted membrane delivery and polarization of the elongating cysts.
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