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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2005-5-16
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pubmed:abstractText |
Nectins are immunoglobulin superfamily adhesion molecules that participate in the organization of epithelial and endothelial junctions. Sharing high homology with the poliovirus receptor (PVR/CD155), nectins were also named poliovirus receptor-related proteins (PRRs). Four nectins and five nectin-like molecules have been identified. Here we describe the cloning and characterization of human and mouse nectin-like molecular 1 (NECL1). Human and mouse NECL1 share 87.3% identity at the amino acid level. NECL1 contains an ectodomain made of three immunoglobulin-like domains, and a cytoplasmic region homologous to those of glycophorin C and contactin-associated protein. RNA blot and in situ hybridization analysis showed that NECL1 predominantly expressed in the central nervous system, mainly in neuronal cell bodies in a variety of brain regions including the cerebellum, cerebral cortex and hippocampus. In vitro binding assay proved the association of NECL1 with protein 4.1N. NECL1 localizes to the cell-cell junctions and recruits protein 4.1N to the plasma membranes through its C-terminus, thus may regulate the function of the cell-cell junction. We propose that the NECL1 and protein 4.1N complex is involved in the morphological development, stability, and dynamic plasticity of the nervous system.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Blood Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/CADM1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Microtubule-Associated Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neuropeptides,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/cell adhesion molecule 1, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/erythrocyte membrane band 4.1...,
http://linkedlifedata.com/resource/pubmed/chemical/erythrocyte membrane protein band...
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0006-3002
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pubmed:author |
pubmed-author:DeyD KDK,
pubmed-author:DuGuangweiG,
pubmed-author:FanMingM,
pubmed-author:HuXiaoyanX,
pubmed-author:HuangXiaoweiX,
pubmed-author:LiuYaoboY,
pubmed-author:PengXiaozhongX,
pubmed-author:QiangBoqinB,
pubmed-author:SerýOO,
pubmed-author:SunJ KJK,
pubmed-author:XuYaqinY,
pubmed-author:YuanJiangangJ,
pubmed-author:ZhouYanY
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pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
1669
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
142-54
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pubmed:dateRevised |
2011-8-23
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pubmed:meshHeading |
pubmed-meshheading:15893517-Amino Acid Sequence,
pubmed-meshheading:15893517-Animals,
pubmed-meshheading:15893517-Blood Proteins,
pubmed-meshheading:15893517-Blotting, Western,
pubmed-meshheading:15893517-Cell Adhesion Molecules,
pubmed-meshheading:15893517-Cell Membrane,
pubmed-meshheading:15893517-Central Nervous System,
pubmed-meshheading:15893517-Cytoplasm,
pubmed-meshheading:15893517-Cytoskeletal Proteins,
pubmed-meshheading:15893517-Humans,
pubmed-meshheading:15893517-Immunoglobulins,
pubmed-meshheading:15893517-Membrane Proteins,
pubmed-meshheading:15893517-Mice,
pubmed-meshheading:15893517-Microtubule-Associated Proteins,
pubmed-meshheading:15893517-Molecular Sequence Data,
pubmed-meshheading:15893517-Neuropeptides,
pubmed-meshheading:15893517-RNA, Messenger,
pubmed-meshheading:15893517-Sequence Alignment,
pubmed-meshheading:15893517-Sequence Analysis, Protein,
pubmed-meshheading:15893517-Tumor Suppressor Proteins
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pubmed:year |
2005
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pubmed:articleTitle |
Nectin-like molecule 1 is a protein 4.1N associated protein and recruits protein 4.1N from cytoplasm to the plasma membrane.
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pubmed:affiliation |
National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences and Peking Union Medical College, National Human Genome Center, Beijing 100005, China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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