MTORC1 and muscle regeneration are regulated by the LINC00961-encoded SPAR polypeptide

Nature

Volumn 541, Issue 7636, 2017, Pages 228-232

  Matsumoto, Akinobu ^a   Pasut, Alessandra ^a   Matsumoto, Masaki ^b   Yamashita, Riu ^c   Fung, Jacqueline ^a   Monteleone, Emanuele ^a,d   Saghatelian, Alan ^e   Nakayama, Keiichi I ^b   Clohessy, John G ^a   Pandolfi, Pier Paolo ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

^b KYUSHU UNIVERSITY   (Japan)

^c TOHOKU UNIVERSITY   (Japan)

^d UNIVERSITY OF TURIN   (Italy)

^e SALK INSTITUTE FOR BIOLOGICAL STUDIES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; LONG UNTRANSLATED RNA; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; POLYPEPTIDE; SERYLPROLYLALANYLARGININE; UNCLASSIFIED DRUG; AMINO ACID; MECHANISTIC TARGET OF RAPAMYCIN COMPLEX 1; MULTIPROTEIN COMPLEX; PEPTIDE; SPAR POLYPEPTIDE, HUMAN; SPAR POLYPEPTIDE, MOUSE; TARGET OF RAPAMYCIN KINASE;

AMINO ACID; ENZYME ACTIVITY; GENE EXPRESSION; HOMINID; MUSCLE; PEPTIDE; PROTEIN; REGENERATION; RODENT;

ANIMAL EXPERIMENT; ARTICLE; CONTROLLED STUDY; CRISPR CAS SYSTEM; ENDOSOME; FEMALE; HEK293 CELL LINE; HELA CELL LINE; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; IN VITRO STUDY; LYSOSOME; MOUSE; MUSCLE REGENERATION; MYOBLAST; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SKELETAL MUSCLE; AGONISTS; ANIMAL; ANTIBODY SPECIFICITY; DEFICIENCY; DRUG EFFECTS; ENZYMOLOGY; GENE EDITING; GENETICS; INJURIES; MALE; METABOLISM; MUSCLE; PHYSIOLOGY; REGENERATION; SIGNAL TRANSDUCTION;

ADENOSINE TRIPHOSPHATASES; AMINO ACIDS; ANIMALS; CRISPR-CAS SYSTEMS; ENDOSOMES; GENE EDITING; HEK293 CELLS; HUMANS; LYSOSOMES; MALE; MICE; MULTIPROTEIN COMPLEXES; MUSCLES; ORGAN SPECIFICITY; PEPTIDES; REGENERATION; RNA, LONG NONCODING; SIGNAL TRANSDUCTION; TOR SERINE-THREONINE KINASES;

EID: 85016138431     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature21034     Document Type: Article

References (24)

1. Ingolia, N. T., Lareau, L. F., Weissman, J. S. Ribosome profiling of mouse embryonic stem cells reveals the complexity and dynamics of mammalian proteomes. Cell 147, 789-802 (2011).
2. Kim, M. S., et al. A draft map of the human proteome. Nature 509, 575-581 (2014).
3. Slavoff, S. A., et al. Peptidomic discovery of short open reading frame-encoded peptides in human cells. Nat. Chem. Biol. 9, 59-64 (2013).
4. Birney, E., et al. Identification and analysis of functional elements in 1% of the human genome by the ENCODE pilot project. Nature 447, 799-816 (2007).
5. Carninci, P., et al. The transcriptional landscape of the mammalian genome. Science 309, 1559-1563 (2005).
6. Derrien, T., et al. The GENCODE v7 catalog of human long noncoding RNAs: analysis of their gene structure, evolution, expression. Genome Res. 22, 1775-1789 (2012).
7. Pauli, A., et al. Toddler: an embryonic signal that promotes cell movement via Apelin receptors. Science 343, 1248636 (2014).
8. Kondo, T., et al. Small peptides switch the transcriptional activity of Shavenbaby during Drosophila embryogenesis. Science 329, 336-339 (2010).
9. Magny, E. G., et al. Conserved regulation of cardiac calcium uptake by peptides encoded in small open reading frames. Science 341, 1116-1120 (2013).
10. Anderson, D. M., et al. A micropeptide encoded by a putative long noncoding RNA regulates muscle performance. Cell 160, 595-606 (2015).
11. Nelson, B. R., et al. A peptide encoded by a transcript annotated as long noncoding RNA enhances SERCA activity in muscle. Science 351, 271-275 (2016).
12. Cabili, M. N., et al. Integrative annotation of human large intergenic noncoding RNAs reveals global properties and specific subclasses. Genes Dev. 25, 1915-1927 (2011).
13. Humphries, W. H., IV, Szymanski, C. J., Payne, C. K. Endo-lysosomal vesicles positive for Rab7 and LAMP1 are terminal vesicles for the transport of dextran. PLoS One 6, e26626 (2011).
14. Rebsamen, M., et al. SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1. Nature 519, 477-481 (2015).
15. Zoncu, R., et al. mTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H+ATPase. Science 334, 678-683 (2011).
16. Bar-Peled, L., Sabatini, D. M. Regulation of mTORC1 by amino acids. Trends Cell Biol. 24, 400-406 (2014).
17. Sancak, Y., et al. Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids. Cell 141, 290-303 (2010).
18. Sancak, Y., et al. The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1. Science 320, 1496-1501 (2008).
19. Bar-Peled, L., Schweitzer, L. D., Zoncu, R., Sabatini, D. M. Ragulator is a GEF for the rag GTPases that signal amino acid levels to mTORC1. Cell 150, 1196-1208 (2012).
20. Bentzinger, C. F., et al. Skeletal muscle-specific ablation of raptor, but not of rictor, causes metabolic changes and results in muscle dystrophy. Cell Metab. 8, 411-424 (2008).
21. Ge, Y., et al. mTOR regulates skeletal muscle regeneration in vivo through kinase-dependent and kinase-independent mechanisms. Am. J. Physiol. Cell Physiol. 297, C1434-C1444 (2009).
22. Pereira, M. G., et al. Leucine supplementation accelerates connective tissue repair of injured tibialis anterior muscle. Nutrients 6, 3981-4001 (2014).
23. Zhang, P., et al. mTOR is necessary for proper satellite cell activity and skeletal muscle regeneration. Biochem. Biophys. Res. Commun. 463, 102-108 (2015).
24. Li Chew, C., et al. In vivo role of INPP4B in tumor and metastasis suppression through regulation of PI3K-AKT signaling at endosomes. Cancer Discov. 5, 740-751 (2015).