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

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

Stable Identifier

R-HSA-6784676

Type

Reaction [transition]

Species

Homo sapiens

Compartment

plasma membrane, extracellular region

ReviewStatus

5/5

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

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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
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
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