PCSK5 mediates dissociation of 2 x LPL from GPIHBP1:HSPG:LPL dimer

Stable Identifier
R-HSA-6784676
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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LPL enzyme is catalytically active as a dimer composed of two glycosylated subunits of LPL connected in a head-to-tail arrangement by non-covalent interactions. Dimeric LPL is cleaved by several proprotein convertases. Proprotein convertase subtilisin/kexin type 5 (PCSK5) can cleave LPL dimer, inactivating it, resulting in subsequent increase in plasma TG concentrations (Paule et al. 2012). ANGPTL4 binds transiently to LPL dimer, the interaction resulting in conversion of the enzyme from a catalytically active dimer to inactive, but still folded, monomers (Sukonina et al. 2006).

Literature References
PubMed ID Title Journal Year
22740495 Cleavage of endometrial α-integrins into their functional forms is mediated by proprotein convertase 5/6

Paule, S, Aljofan, M, Simón, C, Rombauts, LJ, Nie, G

Hum. Reprod. 2012
17088546 Angiopoietin-like protein 4 converts lipoprotein lipase to inactive monomers and modulates lipase activity in adipose tissue

Sukonina, V, Lookene, A, Olivecrona, T, Olivecrona, G

Proc. Natl. Acad. Sci. U.S.A. 2006
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
endopeptidase activity of PCSK5 [extracellular region]
Physical Entity
Activity
This event is regulated
Orthologous Events
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Created