A role for Raptor phosphorylation in the mechanical activation of mTOR signaling

Cellular Signalling

Volumn 26, Issue 2, 2014, Pages 313-322

  Frey, John W ^a   Jacobs, Brittany L ^a   Goodman, Craig A ^a   Hornberger, Troy A ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

Exercise; Hypertrophy; Mechanotransduction; MTOR; Raptor; Skeletal muscle

Indexed keywords

CELL PROTEIN; MAMMALIAN TARGET OF RAPAMYCIN; PROLINE; RAPTOR PROTEIN; S6 KINASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; ECCENTRIC MUSCLE CONTRACTION; ELECTROPORATION; IMMUNOPRECIPITATION; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; MECHANICAL STIMULATION; MOUSE; MUSCLE CONTRACTION; MUSCLE MASS; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN PHOSPHORYLATION; SIGNAL TRANSDUCTION; SKELETAL MUSCLE; WESTERN BLOTTING;

C-JUN N-TERMINAL KINASE; EC; ECCENTRIC CONTRACTION; EXERCISE; G-PROTEIN Β-SUBUNIT-LIKE PROTEIN; GFP; GREEN FLUORESCENT PROTEIN; GΒL; HYPERTROPHY; JNK; LETHAL WITH SEC13 PROTEIN 8; MAMMALIAN [OR MECHANISTIC] TARGET OF RAPAMYCIN; MAPK; MECHANOTRANSDUCTION; MITOGEN-ACTIVATED PROTEIN KINASE; MLST8; MTOR; MTOR COMPLEX 1; MTOR COMPLEX 2; MTORC1; MTORC2; P38; P38 MITOGEN-ACTIVATED PROTEIN KINASE; P70(S6K); PHOSPHOTIDYLINOSITOL-3-KINASE; PI3K; PRAS40; PROLINE-RICH AKT SUBSTRATE OF 40KDA; RAPTOR; REGULATORY ASSOCIATED PROTEIN OF MTOR; RIBOSOMAL S6 KINASE 1; SKELETAL MUSCLE; TA; TIBIALIS ANTERIOR MUSCLE;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; ANTI-BACTERIAL AGENTS; MASS SPECTROMETRY; MICE; MICE, INBRED C57BL; MOLECULAR SEQUENCE DATA; MUSCLE, SKELETAL; PHOSPHOPEPTIDES; PHOSPHOPROTEINS; PHOSPHORYLATION; PROTEIN BINDING; RIBOSOMAL PROTEIN S6 KINASES, 70-KDA; SIGNAL TRANSDUCTION; SIROLIMUS; STRESS, MECHANICAL; TOR SERINE-THREONINE KINASES;

EID: 84889644629     PISSN: 08986568     EISSN: 18733913     Source Type: Journal    
DOI: 10.1016/j.cellsig.2013.11.009     Document Type: Article

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