Source:http://linkedlifedata.com/resource/pubmed/id/12042308
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
33
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pubmed:dateCreated |
2002-8-12
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pubmed:abstractText |
In an attempt to find podocyte-expressed proteins that may interact with the tight junction protein MAGI-1, we screened a glomerulus-enriched cDNA library with a probe consisting of both WW domains of MAGI-1. One of the isolated clones contained two WW domain-binding motifs and was identified as a portion of the actin-bundling protein synaptopodin. In vitro binding assays confirmed this interaction between MAGI-1 and synaptopodin and identified the second WW domain of MAGI-1 to be responsible for the interaction. MAGI-1 and synaptopodin can also interact in vivo, as they can be immunoprecipitated together from HEK293 cell lysates. Another actin-bundling protein that is found in glomerular podocytes and shown to be mutated in an inheritable form of glomerulosclerosis is alpha-actinin-4. We show that alpha-actinin-4 is also capable of binding to MAGI-1 in in vitro binding assays and that this interaction is mediated by the fifth PDZ domain of MAGI-1 binding to the C terminus of alpha-actinin-4. Exogenously expressed synaptopodin and alpha-actinin-4 were found to colocalize along with endogenous MAGI-1 at the tight junction of Madin-Darby canine kidney cells. The interaction and colocalization of MAGI-1 with two actin-bundling proteins suggest that MAGI-1 may play a role in actin cytoskeleton dynamics within polarized epithelial cells.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actinin,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Guanylate Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleoside-Phosphate Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/SYNPO protein, human
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
277
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
30183-90
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12042308-Actinin,
pubmed-meshheading:12042308-Animals,
pubmed-meshheading:12042308-Base Sequence,
pubmed-meshheading:12042308-Cell Line,
pubmed-meshheading:12042308-DNA Primers,
pubmed-meshheading:12042308-Dogs,
pubmed-meshheading:12042308-Fluorescent Antibody Technique,
pubmed-meshheading:12042308-Guanylate Kinase,
pubmed-meshheading:12042308-Humans,
pubmed-meshheading:12042308-Microfilament Proteins,
pubmed-meshheading:12042308-Nucleoside-Phosphate Kinase,
pubmed-meshheading:12042308-Protein Binding
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pubmed:year |
2002
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pubmed:articleTitle |
Interaction of two actin-binding proteins, synaptopodin and alpha-actinin-4, with the tight junction protein MAGI-1.
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pubmed:affiliation |
Department of Internal Medicine, University of Michigan, Ann Arbor, Michigan, 48109-0650, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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