Tissue-specific alternative splicing separates the catalytic and cell signaling functions of human leucyl-tRNA synthetase.

Baymiller, Max; Nordick, Benjamin; Forsyth, Connor M; Martinis, Susan A

Baymiller, Max; Nordick, Benjamin; Forsyth, Connor M; Martinis, Susan A.

Affiliation

Baymiller M; Department of Biochemistry, University of Illinois Urbana-Champaign, Urbana, Illinois, USA.
Nordick B; Department of Biochemistry, University of Illinois Urbana-Champaign, Urbana, Illinois, USA.
Forsyth CM; Department of Biochemistry, University of Illinois Urbana-Champaign, Urbana, Illinois, USA.
Martinis SA; Department of Biochemistry, University of Illinois Urbana-Champaign, Urbana, Illinois, USA. Electronic address: martinis@illinois.edu.

J Biol Chem ; 298(4): 101757, 2022 04.

Article in En | MEDLINE | ID: mdl-35202654

Subject(s)

Alternative Splicing; Leucine-tRNA Ligase; Humans; Leucine-tRNA Ligase/genetics; Leucine-tRNA Ligase/metabolism; RNA, Transfer/metabolism; Serine-Arginine Splicing Factors/metabolism; Signal Transduction; TOR Serine-Threonine Kinases/metabolism

Key words

alternative splicing; aminoacyl-tRNA synthetase; mammalian target of rapamycin (mTOR); serine/arginine-rich splicing factor 1 (SRSF1); transfer RNA (tRNA); translation

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Alternative Splicing / Leucine-tRNA Ligase Limits: Humans Language: En Journal: J Biol Chem Year: 2022 Document type: Article Affiliation country: United States Country of publication: United States

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