Cloning of a novel kinase (SIK) of the SNF1/AMPK family from high salt diet‐treated rat adrenal1

• Published in: FEBS letters Vol. 453; no. 1-2; pp. 135 - 139
• Main Authors: Wang, Zhi-nong, Takemori, Hiroshi, Halder, Sunil K, Nonaka, Yasuki, Okamoto, Mitsuhiro
• Format: Journal Article
• Language: English
• Published: 18.06.1999
• Subjects: ACTH, adrenocorticotropic hormone; Adrenocortical function; Adrenocorticotropic hormone; AII, angiotensin II; AMPK, AMP-activated protein kinase; G3PDH, glyceraldehyde 3-phosphate dehydrogenase; GST, glutathione S-transferase; PCR, polymerase chain reaction; PKA, cAMP-dependent protein kinase; PKC, calcium/phospholipid-dependent protein kinase; Protein serine/threonine kinase; RACE, rapid amplification of cDNA ends; Salt inducible kinase; SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electrophoresis; SIK, salt-inducible kinase; SNF1, sucrose-non-fermenting 1 protein kinase; SNF1/AMPK; Y1 mouse adrenocortical tumor cell
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(99)00708-5

PCR‐coupled cDNA subtraction hybridization was adapted to identify the genes expressed in the adrenocortical tissues from high salt diet‐treated rat. A novel cDNA clone, termed alt‐nducible inase (SIK), encoding a polypeptide (776 amino acids) with significant similarity to protein serine/threonine kinases in the SNF1/AMPK family was isolated. An in vitro kinase assay demonstrated that SIK protein had autophosphorylation activity. Northern blot revealed that SIK mRNA levels were markedly augmented by ACTH treatment both in rat adrenal glands and in Y1 cells. SIK may play an important role in the regulation of adrenocortical functions in response to high plasma salt and ACTH stimulation.