A truncated isoform of Ca2+/calmodulin‐dependent protein kinase II expressed in human islets of Langerhans may result from trans‐splicing

FEBS Letters

Ashcroft, Stephen J.H.¹  Breen, Maria A.¹ 

[1] Nuffield Department of Clinical Biochemistry, John Radcliffe Hospital, Headington, Oxford OX3 9DU, UK

关键词: CaM kinase II;    Signal recognition particle;    Trans-splicing;    Pancreatic β-cell;    Human islets of Langerhans;    Protein phosphorylation;    CaM kinase II;    calcium/calmodulin-dependent protein kinase II;    RACE;    rapid amplification of cDNA ends;    SRP72;    the gene coding for the 72-kDa protein of the signal recognition particle;   

DOI  :  10.1016/S0014-5793(97)00555-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Calcium/calmodulin-dependent protein kinase II (CaM kinase II) has been proposed to play a key role in glucose stimulated insulin secretion. Using the rapid amplification of cDNA ends technique we amplified the 3′ end of the CaM kinase II γ gene from human islet RNA. A novel cDNA was detected composed of 5′ sequence from the human CaM kinase II γ gene joined to the 3′ end of the human signal recognition particle 72 (SRP72) gene. We predict that this mRNA species will code for a truncated form of CaM kinase II, designated γ_SRP, comprising the entire catalytic and regulatory domains of the protein and with a predicted molecular weight of 37 kDa. We mapped the human SRP72 gene to chromosome 18 and, as the CaM kinase II γ gene was previously mapped to human chromosome 10q22, we suggest this novel cDNA may have resulted from trans-splicing.

【 授权许可】

Unknown