The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit.
- 1 April 1993
- journal article
- Published by Cold Spring Harbor Laboratory in Genes & Development
- Vol. 7 (4) , 555-569
- https://doi.org/10.1101/gad.7.4.555
Abstract
The retinoblastoma protein (p110RB) interacts with many cellular proteins in complexes potentially important for its growth-suppressing function. We have developed and used an improved version of the yeast two-hybrid system to isolate human cDNAs encoding proteins able to bind p110RB. One clone encodes a novel type 1 protein phosphatase catalytic subunit (PP-1 alpha 2), which differs from the originally defined PP-1 alpha by an amino-terminal 11-amino-acid insert. In vitro-binding assays demonstrated that PP-1 alpha isoforms preferentially bind the hypophosphorylated form of p110RB. Moreover, similar p110RB sequences are required for binding PP-1 alpha 2 and SV40 large T antigen. Cell cycle synchrony experiments revealed that this association occurs from mitosis to early G1. The implications of these findings on the regulation of both proteins are discussed.Keywords
This publication has 73 references indexed in Scilit:
- A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformaion of Escherichia coliPublished by Elsevier ,2003
- Protein phosphatase type 1 in mammalian cell mitosis: chromosomal localization and involvement in mitotic exit.The Journal of cell biology, 1992
- G1/S phosphorylation of the retinoblastoma protein is associated with an altered affinity for the nuclear compartmentCell, 1991
- A cellular protein that competes with SV40 T antigen for binding to the retinoblastoma gene productNature, 1991
- Protein serine/threonine phosphatases; an expanding familyFEBS Letters, 1990
- The product of the retinoblastoma susceptibility gene has properties of a cell cycle regulatory elementCell, 1989
- Phosphorylation of the retinoblastoma gene product is modulated during the cell cycle and cellular differentiationCell, 1989
- A novel genetic system to detect protein–protein interactionsNature, 1989
- Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferaseGene, 1988
- Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mpl8 and pUC19 vectorsGene, 1985