Ribosomal RACK1:Protein Kinase C βII Modulates Intramolecular Interactions between Unstructured Regions of Eukaryotic Initiation Factor 4G (eIF4G) That Control eIF4E and eIF3 Binding | Zendy

Mikhail I. Dobrikov | Zendy; Elena Y. Dobrikova | Zendy; Matthias Gromeier | Zendy

Open Access

Ribosomal RACK1:Protein Kinase C βII Modulates Intramolecular Interactions between Unstructured Regions of Eukaryotic Initiation Factor 4G (eIF4G) That Control eIF4E and eIF3 Binding

Author(s) -

Mikhail I. Dobrikov,

Elena Y. Dobrikova,

Matthias Gromeier

Publication year - 2018

Publication title -

molecular and cellular biology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.14

H-Index - 327

eISSN - 1067-8824

pISSN - 0270-7306

DOI - 10.1128/mcb.00306-18

Subject(s) - eif4g , biology , eukaryotic initiation factor , eif4e , microbiology and biotechnology , eukaryotic small ribosomal subunit , protein kinase c , initiation factor , eukaryotic translation , kinase , biochemistry , translation (biology) , messenger rna , gene

The receptor for activated C kinase (RACK1), a conserved constituent of eukaryotic ribosomes, mediates phosphorylation of eukaryotic initiation factor 4G1(S1093) [eIF4G1(S1093)] and eIF3a(S1364) by protein kinase C βII (PKCβII) (M. I.

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