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Translation of insulin granule proteins are regulated by PDI and PABP.
Sarwade, Rucha D; Khalique, Abdul; Kulkarni, Shardul D; Pandey, Poonam R; Gaikwad, Naina; Seshadri, Vasudevan.
Afiliação
  • Sarwade RD; National Centre of Cell Science, Ganeshkhind, Pune, 411007, India; Savitribai Phule Pune University, Ganeshkhind, Pune, 411007, India.
  • Khalique A; National Centre of Cell Science, Ganeshkhind, Pune, 411007, India; Savitribai Phule Pune University, Ganeshkhind, Pune, 411007, India.
  • Kulkarni SD; National Centre of Cell Science, Ganeshkhind, Pune, 411007, India; Savitribai Phule Pune University, Ganeshkhind, Pune, 411007, India.
  • Pandey PR; National Centre of Cell Science, Ganeshkhind, Pune, 411007, India; Savitribai Phule Pune University, Ganeshkhind, Pune, 411007, India.
  • Gaikwad N; National Centre of Cell Science, Ganeshkhind, Pune, 411007, India; Savitribai Phule Pune University, Ganeshkhind, Pune, 411007, India.
  • Seshadri V; National Centre of Cell Science, Ganeshkhind, Pune, 411007, India. Electronic address: seshadriv@nccs.res.in.
Biochem Biophys Res Commun ; 526(3): 618-625, 2020 06 04.
Article em En | MEDLINE | ID: mdl-32248978
ABSTRACT
Glucose mediated insulin biosynthesis is tightly regulated and shared between insulin granule proteins such as its processing enzymes, prohormone convertases, PC1/3 and PC2. However, the molecular players involved in the co-ordinated translation remain elusive. The trans-acting factors like PABP (Poly A Binding Protein) and PDI (Protein Disulphide Isomerize) binds to a conserved sequence in the 5'UTR of insulin mRNA and regulates its translation. Here, we demonstrate that 5'UTR of PC1/3 and PC2 also associate with PDI and PABP. We show that a' and RRM 3-4 domains of PDI and PABP respectively, are necessary for RNA binding activity to the 5'UTRs of insulin and its processing enzymes.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Biossíntese de Proteínas / Isomerases de Dissulfetos de Proteínas / Proteínas de Ligação a Poli(A) / Pró-Proteína Convertase 1 / Pró-Proteína Convertase 2 / Insulina Limite: Animals Idioma: En Revista: Biochem Biophys Res Commun Ano de publicação: 2020 Tipo de documento: Article País de afiliação: Índia

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Biossíntese de Proteínas / Isomerases de Dissulfetos de Proteínas / Proteínas de Ligação a Poli(A) / Pró-Proteína Convertase 1 / Pró-Proteína Convertase 2 / Insulina Limite: Animals Idioma: En Revista: Biochem Biophys Res Commun Ano de publicação: 2020 Tipo de documento: Article País de afiliação: Índia