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The Proprotein Convertase (PC) PCSK9 Is Inactivated by Furin and/or PC5/6A

Benjannet, Suzanne, Rhainds, David, Hamelin, Josée, Nassoury, Nasha, Seidah, Nabil G.·2006·Journal of Biological Chemistry
DOI 10.1074/jbc.m606495200
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Crossref · 10.1074/jbc.m606495200

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  • The proteolytic activity of PCSK9 requires a catalytic triad of Asp186, His226, and Ser386.

    “The proteolytic activity of PCSK9 requires a triad of residues (Asp 186, His 226 and Ser 386), which constitute the 'catalytic triad' of the protease.”

    From PCSK9 is required for the disposal of non-acetylated intermediates of the nascent membrane protein BACE1 (2008) · cites this paper as Benjannet et al, 2006

    The paper identifies Asp186 as an active-site residue in its discussion of furin-cleaved PCSK9 and reports in the Results that the H226A active-site mutant is inactive. Our copy does not identify Ser386 as the third residue or state that these three residues form a catalytic triad required for proteolytic activity (searched: Ser386, catalytic triad). Page numbers were not available in the indexed passages. (LLM, conf=0.85)

    Experimental — accuracy not yet measured

  • Mutation of one residue of the PCSK9 catalytic triad abolishes its proteolytic activity and its ability to undergo processing to the C-form.

    “Mutation of one of these residues abolishes the proteolytic activity of PCSK9 and its ability to undergo processing to the C-form (Benjannet et al, 2004(Benjannet et al, , 2006;;McNutt et al, 2007).”

    From PCSK9 is required for the disposal of non-acetylated intermediates of the nascent membrane protein BACE1 (2008) · cites this paper as Benjannet et al, 2006

    The Results (page unavailable) identify H226A as an active-site mutant that remains in the ER as pro-PCSK9, supporting a failure of normal autocatalytic processing. The cited paper does not call the missing product the “C-form” or directly show that this mutation abolishes PCSK9’s proteolytic activity. (LLM, conf=0.78)

    Experimental — accuracy not yet measured

  • Furin can cleave and inactivate PCSK9 in liver hepatocytes.

    “It can also cleave and inactivate PCSK9 in liver hepatocytes (29, 30).”

    From Asialoglycoprotein receptor 1 is a novel PCSK9-independent ligand of liver LDLR cleaved by furin (2021) · cites this paper as [29]

    The paper states that furin cleaves and inactivates PCSK9 and reports evidence from hepatic HepG2 cells (passage [1], labeled Abstract in our copy). It does not directly demonstrate that cleavage and inactivation occur in liver hepatocytes; its discussion says liver-furin knockout evidence was not available. (LLM, conf=0.84)

    Experimental — accuracy not yet measured

  • PCSK9 can dispose of LDLr in the endosomal-lysosomal compartment.

    “Studies performed with the low-density lipoprotein receptor (LDLr) indicate that PCSK9 can dispose of LDLr both in the 'post-ER compartment' of the secretory pathway (Maxwell & Breslow, 2004;Maxwell et al, 2005) and in the 'endosomal-lysosomal compartment' (Benjannet et al, 2006).”

    From PCSK9 is required for the disposal of non-acetylated intermediates of the nascent membrane protein BACE1 (2008) · cites this paper as Benjannet et al, 2006

  • Insertion of an optimal Furin-like site RRRR103 down arrow EL resulted in complete cleavage of mature approximately 48-kDa ASGR1 by endogenous Furin into a soluble secreted approximately 28-kDa sASGR1.

    “Indeed, insertion of an optimal Furin-like site RRRR103↓EL (17, 29) resulted in complete cleavage of mature ∼48-kDa ASGR1 (upper band, likely endoH resistant (17)) by endogenous Furin into a soluble secreted ∼28-kDa sASGR1 (Fig. 11D).”

    From Asialoglycoprotein receptor 1 is a novel PCSK9-independent ligand of liver LDLR cleaved by furin (2021) · cites this paper as [29]

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Metadata

Authors
Benjannet, S., Rhainds, D., Hamelin, J., Nassoury, N., & Seidah, N. G.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2006-10
Volume
281
Issue
41
Pages
30561-30572
ISSN
0021-9258
DOI
10.1074/jbc.m606495200
Cited by
263
References
2
Language
en
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