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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0001271,
umls-concept:C0020792,
umls-concept:C0037799,
umls-concept:C0050734,
umls-concept:C1514562,
umls-concept:C1514873,
umls-concept:C1522492,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1704241,
umls-concept:C1711351,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
26
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pubmed:dateCreated |
1996-8-20
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pubmed:abstractText |
Adducin is an actin-binding protein that has been proposed to function as a regulated assembly factor for the spectrin/actin network. This study has addressed the question of the subunit and domains of spectrin required for formation of spectrin/adducin/actin complexes in in vitro assays. Quantitative evidence is presented that the beta-spectrin N-terminal domain plus the first two alpha-helical domains are required for optimal participation of spectrin in spectrin/adducin/actin complexes. The alpha subunit exhibited no detectable activity either alone or following association with beta-spectrin. The critical domains of beta-spectrin involved in complex formation were determined using recombinant proteins expressed in bacteria. The N-terminal domain (residues 1-313) of beta-spectrin associated with F-actin with a Kd of 26 microM, and promoted adducin binding to F-actin with half-maximal activation at 110 nM. Addition of the first alpha-helical domain (residues 1-422) lowered the Kdfor F-actin by 4-fold to 6 microM, but also reduced the capacity by 3-fold and had no effect on interaction with adducin. Further addition of the second alpha-helical domain (residues 1-528) did not alter binding to F-actin but resulted in a 2-fold increased activity in promoting adducin binding with half-maximal activation at 50 nM. Addition of up to eight additional alpha-helical domains (residues 1-1388) resulted in no further change in F-actin binding or association with adducin. These results demonstrate an unanticipated role of the first repeat of beta-spectrin in actin binding activity and of the second repeat in association with adducin/actin, and imply the possibility of an extended contact between adducin, spectrin, and actin involving several actin subunits.
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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/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Spectrin,
http://linkedlifedata.com/resource/pubmed/chemical/adducin
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:volume |
271
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
15695-702
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8663089-Actins,
pubmed-meshheading:8663089-Animals,
pubmed-meshheading:8663089-Calmodulin-Binding Proteins,
pubmed-meshheading:8663089-Cattle,
pubmed-meshheading:8663089-Chickens,
pubmed-meshheading:8663089-Macromolecular Substances,
pubmed-meshheading:8663089-Protein Binding,
pubmed-meshheading:8663089-Rabbits,
pubmed-meshheading:8663089-Spectrin,
pubmed-meshheading:8663089-Structure-Activity Relationship
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pubmed:year |
1996
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pubmed:articleTitle |
Identification of the spectrin subunit and domains required for formation of spectrin/adducin/actin complexes.
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pubmed:affiliation |
Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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