Open AccessFunctional interactions between polypyrimidine tract binding protein and PRI peptide ligand containing proteins
Author(s) -
Miguel B. Coelho,
David B. Ascher,
Clare Gooding,
Emma Lång,
Hannah Maude,
David A. Turner,
Miriam Llorian,
Douglas E. V. Pires,
Jan Attig,
Christopher W. J. Smith
Publication year - 2016
Publication title -
biochemical society transactions
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.562
H-Index - 144
eISSN - 1470-8752
pISSN - 0300-5127
DOI - 10.1042/bst20160080
Subject(s) - polypyrimidine tract binding protein , heterogeneous ribonucleoprotein particle , rna binding protein , ribonucleoprotein , heterogeneous nuclear ribonucleoprotein , rna , rna recognition motif , microbiology and biotechnology , chemistry , polypyrimidine tract , biology , biochemistry , gene
Polypyrimidine tract binding protein (PTBP1) is a heterogeneous nuclear ribonucleoprotein (hnRNP) that plays roles in most stages of the life-cycle of pre-mRNA and mRNAs in the nucleus and cytoplasm. PTBP1 has four RNA binding domains of the RNA recognition motif (RRM) family, each of which can bind to pyrimidine motifs. In addition, RRM2 can interact via its dorsal surface with proteins containing short peptide ligands known as PTB RRM2 interacting (PRI) motifs, originally found in the protein Raver1. Here we review our recent progress in understanding the interactions of PTB with RNA and with various proteins containing PRI ligands.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom