Reaction: PCSK5 mediates dissociation of 2 x LPL from GPIHBP1:HSPG:LPL dimer
- in pathway: Assembly of active LPL and LIPC lipase complexes
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).
Reaction - small molecule participants:
HSPG [plasma membrane]
Reactome.org reaction link: R-HSA-6784676
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Reaction input - small molecules:
Reaction output - small molecules:
heparan sulfate proteoglycan
Reactome.org link: R-HSA-6784676