Cited by 166Autophagy in Disease and TherapyMuscle Physiology and DisordersLipid metabolism and biosynthesis

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Lipin-1 Regulates Autophagy Clearance and Intersects with Statin Drug Effects in Skeletal Muscle

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Zhang, Peixiang, Verity, M. Anthony, Reue, Karen·2014·Cell Metabolism

DOI 10.1016/j.cmet.2014.05.003PMC PMC4170588

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Abstract

LPIN1 encodes lipin-1, a phosphatidic acid phosphatase (PAP) enzyme that catalyzes the dephosphorylation of phosphatidic acid to form diacylglycerol. Homozygous LPIN1 gene mutations cause severe rhabdomyolysis, and heterozygous LPIN1 missense mutations may promote statin-induced myopathy. We demonstrate that lipin-1-related myopathy in the mouse is associated with a blockade in autophagic flux and accumulation of aberrant mitochondria. Lipin-1 PAP activity is required for maturation of autolysosomes, through its activation of the protein kinase D (PKD)-Vps34 phosphatidylinositol 3-kinase signaling cascade. Statin treatment also reduces PKD activation and autophagic flux, which are compounded by diminished mammalian target of rapamycin (mTOR) abundance in lipin-1-haploinsufficent and -deficient muscle. Lipin-1 restoration in skeletal muscle prevents myonecrosis and statin toxicity in vivo, and activated PKD rescues autophagic flux in lipin-1-deficient cells. Our findings identify lipin-1 PAP activity as a component of the macroautophagy pathway and define the basis for lipin-1-related myopathies.

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Authors: Zhang, P., Verity, M. A., & Reue, K.
Affiliations: University of California, Los Angeles (US)
Corresponding author: Reue, Karen
ORCID: Zhang, Peixiang
Reue, Karen
Venue: Cell Metabolism
Publisher: Elsevier BV
Published: 2014-08
Volume: 20
Issue: 2
Pages: 267-279
ISSN: 1550-4131 (ISSN-L)
DOI: 10.1016/j.cmet.2014.05.003
PMC: PMC4170588
OpenAlex: W2052660293
Cited by: 166
References: 60
Citations by year: 2026: 8 · 2025: 10 · 2024: 20 · 2023: 10 · 2022: 10 · 2021: 18 · 2020: 17 · 2019: 15 · 2018: 16 · 2017: 8 · 2016: 11 · 2015: 19 · 2014: 4
FWCI: 10.58
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 369 d)
Locations: Cell Metabolism (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
eScholarship (California Digital Library) (submittedVersion)
Funders: National Institutes of Health (P01 HL090553, P01 HL028481, P20RR16475)
National Science Foundation (0920663, MCB 0455318, DBI 0521587, EPS 0236913)
Kansas State University
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
Keywords: LPIN1, autophagy, statin-induced myopathy, skeletal muscle, phosphatidate phosphohydrolase, protein kinase D, mTOR, mitochondrial accumulation, muscle necrosis, rhabdomyolysis, macroautophagy, diacylglycerol
MeSH terms: Animals, Autophagy, Cell Line, Creatine Kinase, Female, Lipids, Mice, Inbred BALB C, Microtubule-Associated Proteins, Mitochondria, Nuclear Proteins, Phosphatidate Phosphatase, Protein Kinase C, Muscle, Skeletal, Hydroxymethylglutaryl-CoA Reductase Inhibitors, Mice, Haploinsufficiency, Class III Phosphatidylinositol 3-Kinases, TOR Serine-Threonine Kinases

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Lipin-1 Regulates Autophagy Clearance and Intersects with Statin Drug Effects in Skeletal Muscle

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