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Laminin-511 degradation by MMP14
Stable Identifier
R-HSA-2533874
Type
Reaction [transition]
Species
Homo sapiens
Compartment
plasma membrane
,
extracellular region
ReviewStatus
5/5
Locations in the PathwayBrowser
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Extracellular matrix organization (Homo sapiens)
Degradation of the extracellular matrix (Homo sapiens)
Laminin-511 degradation by MMP14 (Homo sapiens)
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Laminins are an important molecular component of the basement membranes (BMs) in a variety of tissue types. They have a cruciform shape, and are composed of three chains, alpha, beta and gamma., all of which have multiple subtypes. At the ultrastructural level, each laminin trimer appears as a cross-like structure with a large globular domain (LG domain) at the base of the cross. The LG domain is the C-terminal domain of the alpha subunit; it is divided into five homologous subdomains LG1-5 (Sugawara et al. 2008). Laminin-511 (alpha-5 beta-1gamma-1) is a major structural component of many basement membranes (BMs) including the BM that separates the epidermis from the dermis (Määttä et al. 2001). MMP14 (MT1-MMP) has been shown to cleave the alpha chain of laminin-511, promoting tumor cell migration (Bair et al. 2005). Loss of laminin-511 is a likely contributor to age-related hair loss (Pouliot et al. 2002).
Participants
Input
Laminin-511 [extracellular region]
(Homo sapiens)
Output
Laminin-511 (cleaved alpha chain) [extracellular region]
(Homo sapiens)
Participates
as an event of
Degradation of the extracellular matrix (Homo sapiens)
Catalyst Activity
metalloendopeptidase activity of MMP14,TMPRSS6 [plasma membrane]
Physical Entity
MMP14,TMPRSS6 [plasma membrane]
(Homo sapiens)
Activity
metalloendopeptidase activity (GO:0004222)
Inferred From
Laminin-511 degradation by MMP14 (Homo sapiens)
Authored
Jupe, S (2012-08-08)
Reviewed
Ricard-Blum, S (2013-08-13)
Created
Jupe, S (2012-10-22)
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