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Shim, Sang-Hee
Shim Research Lab
Research Interests
  • Super-resolution Optical Imaging

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Structurally distinct Ca2+ signaling domains of sperm flagella orchestrate tyrosine phosphorylation and motility

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Title
Structurally distinct Ca2+ signaling domains of sperm flagella orchestrate tyrosine phosphorylation and motility
Author
Chung, Jean-JuShim, Sang-HeeEverley, Robert A.Gygi, Steven P.Zhuang, XiaoweiClapham, David E.
Keywords
OPTICAL RECONSTRUCTION MICROSCOPY; SOLUBLE ADENYLYL-CYCLASE; CATSPER2 NULL SPERM; MOUSE SPERMATOZOA; FIBROUS SHEATH; MALE-FERTILITY; PROTEIN-PHOSPHORYLATION; MAMMALIAN SPERMATOZOA; CHANNEL; CAPACITATION
Issue Date
201405
Publisher
CELL PRESS
Citation
CELL, v.157, no.4, pp.808 - 822
Abstract
Spermatozoa must leave one organism, navigate long distances, and deliver their paternal DNA into a mature egg. For successful navigation and delivery, a sperm-specific calcium channel is activated in the mammalian flagellum. The genes encoding this channel (CatSpers) appear first in ancient uniflagellates, suggesting that sperm use adaptive strategies developed long ago for single-cell navigation. Here, using genetics, super-resolution fluorescence microscopy, and phosphoproteomics, we investigate the CatSper-dependent mechanisms underlying this flagellar switch. We find that the CatSper channel is required for four linear calcium domains that organize signaling proteins along the flagella. This unique structure focuses tyrosine phosphorylation in time and space as sperm acquire the capacity to fertilize. In heterogeneous sperm populations, we find unique molecular phenotypes, but only sperm with intact CatSper domains that organize time-dependent and spatially specific protein tyrosine phosphorylation successfully migrate. These findings illuminate flagellar adaptation, signal transduction cascade organization, and fertility.
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DOI
http://dx.doi.org/10.1016/j.cell.2014.02.056
ISSN
0092-8674
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