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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
2007-6-7
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pubmed:databankReference |
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pubmed:abstractText |
The evolutionarily conserved Par-3/Par-6/aPKC complex is essential for the establishment and maintenance of polarity of a wide range of cells. Both Par-3 and Par-6 are PDZ domain containing scaffold proteins capable of binding to polarity regulatory proteins. In addition to three PDZ domains, Par-3 also contains a conserved N-terminal oligomerization domain (NTD) that is essential for proper subapical membrane localization and consequently the functions of Par-3. The molecular basis of NTD-mediated Par-3 membrane localization is poorly understood. Here, we describe the structure of a monomeric form of the Par-3 NTD. Unexpectedly, the domain adopts a PB1-like fold with both type-I and type-II structural features. The Par-3 NTD oligomerizes into helical filaments via front-to-back interactions. We further demonstrate that the NTD-mediated membrane localization of Par-3 in MDCK cells is solely attributed to its oligomerization capacity. The data presented in this study suggest that the Par-3 NTD is likely to facilitate the assembly of higher-order Par-3/Par-6/aPKC complex with increased avidities in targeting the complex to the subapical membrane domain and in binding to other polarity-regulating proteins.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-10212987,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-10591216,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-10830161,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-10934474,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-10934475,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-11483497,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-11483498,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-11516655,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-12526794,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-12545177,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-12580598,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-12614619,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-12629547,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-12756256,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-12853458,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-12887891,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-12906794,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-14675534,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-15027470,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-15140881,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-15177032,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-15213432,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-15213433,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-15590654,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-15723051,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-15723052,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-16280548,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-16474385,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-16525119,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-16927254,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-3345562,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-8248779,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-8521491,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-8744573,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-8898226,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-9008363,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-9345633,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-9716526,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17476308-9757107
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
26
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2786-96
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:17476308-Amino Acid Sequence,
pubmed-meshheading:17476308-Animals,
pubmed-meshheading:17476308-Carrier Proteins,
pubmed-meshheading:17476308-Cell Polarity,
pubmed-meshheading:17476308-Chromatography, Gel,
pubmed-meshheading:17476308-Membrane Proteins,
pubmed-meshheading:17476308-Microscopy, Electron, Transmission,
pubmed-meshheading:17476308-Microscopy, Fluorescence,
pubmed-meshheading:17476308-Models, Molecular,
pubmed-meshheading:17476308-Molecular Sequence Data,
pubmed-meshheading:17476308-Multiprotein Complexes,
pubmed-meshheading:17476308-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:17476308-Protein Conformation,
pubmed-meshheading:17476308-Protein Structure, Tertiary,
pubmed-meshheading:17476308-Rats
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pubmed:year |
2007
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pubmed:articleTitle |
The Par-3 NTD adopts a PB1-like structure required for Par-3 oligomerization and membrane localization.
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pubmed:affiliation |
Department of Biochemistry, Molecular Neuroscience Center, The Hong Kong University of Science and Technology, Kowloon, Hong Kong.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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