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Translation of insulin granule proteins are regulated by PDI and PABP.

Biochem Biophys Res Commun. 2020 Jun 04;526(3):618-625. Epub 2020 Apr 02
Rucha D Sarwade 1 , Abdul Khalique 1 , Shardul D Kulkarni 1 , Poonam R Pandey 1 , Naina Gaikwad 1 , Vasudevan Seshadri 2
Rucha D Sarwade 1 , Abdul Khalique 1 , Shardul D Kulkarni 1 , Poonam R Pandey 1 , Naina Gaikwad 1 , Vasudevan Seshadri 2
+ et al

[No authors listed]

Author information
  • 1 National Centre of Cell Science, Ganeshkhind, Pune, 411007, India; Savitribai Phule Pune University, Ganeshkhind, Pune, 411007, India.
  • 2 National Centre of Cell Science, Ganeshkhind, Pune, 411007, India. Electronic address: seshadriv@nccs.res.in.

摘要


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.

KEYWORDS: Insulin granule proteins, PABP, PDI, Prohormone convertases