SCY1 like pseudokinase 1 (SCYL1)

SCY1 like pseudokinase 1 (SCYL1) is a highly conserved, ubiquitously expressed protein classified as a pseudokinase due to its divergent N-terminal kinase-like domain, which lacks catalytic activity. SCYL1 contains additional HEAT repeats and a C-terminal coiled-coil domain. It primarily functions as a scaffolding and regulatory protein, localizing to the ER-Golgi intermediate compartment (ERGIC), Golgi apparatus, nucleus, and centrosomes. SCYL1 regulates retrograde trafficking of vesicles between the Golgi and endoplasmic reticulum by interacting with COPI coatomer complexes and Golgi-associated proteins and is involved in maintenance of Golgi morphology. Certain isoforms also participate in transcriptional activation of the telomerase reverse transcriptase and DNA polymerase beta genes. SCYL1 plays important roles in RNA metabolism, nucleocytoplasmic transport of tRNAs, and may regulate REST protein turnover. Pathogenic variants in SCYL1 are associated with neurodegenerative disease (including a mouse model of ALS), spinocerebellar ataxia, and syndromes affecting the liver and peripheral nervous system[1][2][3][5][7]. Currently, there are no known therapeutic drugs targeting SCYL1, and it is not considered a typical drug target or receptor.

Other names

N-terminal kinase-like proteinCVAK90GKLPNTKLTAPKTEIFTRAPHT019P105SCAR21telomerase regulation-associated proteintelomerase transcriptional element-interacting factorteratoma-associated tyrosine kinasecoated vesicle-associated kinase of 90 kDaSCY1-like protein 1