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FN1 dimerizes
Stable Identifier
R-HSA-2545196
Type
Reaction [binding]
Species
Homo sapiens
Compartment
extracellular region
Synonyms
Fibronectin dimerizes
ReviewStatus
5/5
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Extracellular matrix organization (Homo sapiens)
Fibronectin matrix formation (Homo sapiens)
FN1 dimerizes (Homo sapiens)
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The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
Prior to matrix formation, fibronectin (FN1) exists as a protein dimer. Often the two peptide chains are differentially-spliced variants. The chains are linked by a pair of C-terminal disulfide bonds which are essential for subsequent multimerization (Schwarzbaur 1991). FN1 monomers have a molecular weight of 230-270 kDa depending on the alternative splicing and contain three types of repeating domains, type I, II, and III. Type I and II domains are stabilized by intra-chain disulfide bonds. FN1 dimer binding to alpha5beta1 integrin stimulates self-association.
Literature References
PubMed ID
Title
Journal
Year
2045422
Identification of the fibronectin sequences required for assembly of a fibrillar matrix
Schwarzbauer, JE
J. Cell Biol.
1991
Participants
Input
x 2
FN1(32-2386) [extracellular region]
(Homo sapiens)
Output
FN1 dimer [extracellular region]
(Homo sapiens)
Participates
as an event of
Fibronectin matrix formation (Homo sapiens)
Orthologous Events
FN1 dimerizes (Bos taurus)
FN1 dimerizes (Caenorhabditis elegans)
FN1 dimerizes (Canis familiaris)
FN1 dimerizes (Dictyostelium discoideum)
FN1 dimerizes (Gallus gallus)
FN1 dimerizes (Mus musculus)
FN1 dimerizes (Rattus norvegicus)
FN1 dimerizes (Sus scrofa)
FN1 dimerizes (Xenopus tropicalis)
Authored
Jupe, S (2011-07-12)
Reviewed
Reinhardt, DP (2013-02-08)
Created
Jupe, S (2012-11-01)
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