Source:http://linkedlifedata.com/resource/pubmed/id/16854985
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
38
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pubmed:dateCreated |
2006-9-18
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pubmed:abstractText |
Sperm-specific phospholipase C-zeta (PLCzeta) causes intracellular Ca(2+) oscillations and thereby egg activation and is accumulated into the formed pronucleus (PN) when expressed in mouse eggs by injection of cRNA encoding PLCzeta, which consists of four EF-hand domains (EF1-EF4) in the N terminus, X and Y catalytic domains, and C-terminal C2 domain. Those activities were analyzed by expressing PLCzeta mutants tagged with fluorescent protein Venus by injection of cRNA into unfertilized eggs or 1-cell embryos after fertilization. Nuclear localization signal (NLS) existed at 374-381 in the X/Y linker region. Nuclear translocation was lost by replacement of Arg(376), Lys(377), Arg(378), Lys(379), or Lys(381) with glutamate, whereas Ca(2+) oscillations were conserved. Nuclear targeting was also absent for point mutation of Lys(299) and/or Lys(301) in the C terminus of X domain, or Trp(13), Phe(14), or Val(18) in the N terminus of EF1. Ca(2+) oscillation-inducing activity was lost by the former mutation and was remarkably inhibited by the latter. A short sequence 374-383 fused with Venus showed active translocation into the nucleus of COS-7 cells, but 296-309 or 1-19 did not. Despite the presence of these special regions, both activities were deprived by deletion of not only EF1 but also EF2-4 or C2 domain. Thus, PLCzeta is driven into the nucleus primarily by the aid of NLS and putative regulatory sites, but coordinated three-dimensional structure, possibly formed by a folding in the X/Y linker and close EF/C2 contact as in PLCdelta1, seems to be required not only for enzymatic activity but also for nuclear translocation ability.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Localization Signals,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoinositide Phospholipase C,
http://linkedlifedata.com/resource/pubmed/chemical/Plcz1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
22
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pubmed:volume |
281
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
27794-805
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:16854985-Active Transport, Cell Nucleus,
pubmed-meshheading:16854985-Animals,
pubmed-meshheading:16854985-Calcium Signaling,
pubmed-meshheading:16854985-Catalytic Domain,
pubmed-meshheading:16854985-Cell Nucleus,
pubmed-meshheading:16854985-Cells, Cultured,
pubmed-meshheading:16854985-Female,
pubmed-meshheading:16854985-Mice,
pubmed-meshheading:16854985-Models, Molecular,
pubmed-meshheading:16854985-Nuclear Localization Signals,
pubmed-meshheading:16854985-Ovum,
pubmed-meshheading:16854985-Phosphoinositide Phospholipase C,
pubmed-meshheading:16854985-Protein Transport,
pubmed-meshheading:16854985-Type C Phospholipases
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pubmed:year |
2006
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pubmed:articleTitle |
The role of X/Y linker region and N-terminal EF-hand domain in nuclear translocation and Ca2+ oscillation-inducing activities of phospholipase Czeta, a mammalian egg-activating factor.
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pubmed:affiliation |
Department of Physiology, Tokyo Women's Medical University School of Medicine, Tokyo 162-8666, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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