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The subcellular locations of p15(Ink4b) and p27(Kip1) coordinate their inhibitory interactions with cdk4 and cdk2.

The subcellular locations of p15(Ink4b) and p27(Kip1) coordinate their inhibitory interactions... Downloaded from genesdev.cshlp.org on December 7, 2021 - Published by Cold Spring Harbor Laboratory Press The subcellular locations of plS^**^"^^ and p27Kipi coordinate their inhibitory interactions with cdk4 and cdk2 Inga Reynisdottir and Joan Massague^ Cell Biology Program and Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, New York, New York 10021 USA In dividing cells, p27^^P^ is predominantly bound to cyclin D-cdk4 without inhibiting this kinase. Upon being induced by TGF-P or with a conditional expression system in lung epithelial cells, plS^"'*'^'' binds to and inhibits the cyclin D-dependent kinases, prevents p27 binding to these cdk complexes, and promotes p27 binding and inhibition of cyclin-cdk2. In vitro, however, pi 5 prevents p27 binding only if it has access to cyclin D-cdk4 first. We present evidence that the different subcellular location of pl 5 and p27 ensures the prior access of pi 5 to cdk4. In the cell, pl 5 is localized mostly in the cytoplasm, whereas p27 is nuclear. pl5 prevails over p27 or a p27 construct consisting of the cdk inhibitory domain tagged with a nuclear localization signal. However, when pl 5 and p27 are forced to reside in the same subcellular location, either the cytoplasm or http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Genes & Development Unpaywall

The subcellular locations of p15(Ink4b) and p27(Kip1) coordinate their inhibitory interactions with cdk4 and cdk2.

Reynisdóttir, I; Massagué, J
Genes & Development – Feb 15, 1997
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Unpaywall
ISSN
0890-9369
DOI
10.1101/gad.11.4.492
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Abstract

Downloaded from genesdev.cshlp.org on December 7, 2021 - Published by Cold Spring Harbor Laboratory Press The subcellular locations of plS^**^"^^ and p27Kipi coordinate their inhibitory interactions with cdk4 and cdk2 Inga Reynisdottir and Joan Massague^ Cell Biology Program and Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, New York, New York 10021 USA In dividing cells, p27^^P^ is predominantly bound to cyclin D-cdk4 without inhibiting this kinase. Upon being induced by TGF-P or with a conditional expression system in lung epithelial cells, plS^"'*'^'' binds to and inhibits the cyclin D-dependent kinases, prevents p27 binding to these cdk complexes, and promotes p27 binding and inhibition of cyclin-cdk2. In vitro, however, pi 5 prevents p27 binding only if it has access to cyclin D-cdk4 first. We present evidence that the different subcellular location of pl 5 and p27 ensures the prior access of pi 5 to cdk4. In the cell, pl 5 is localized mostly in the cytoplasm, whereas p27 is nuclear. pl5 prevails over p27 or a p27 construct consisting of the cdk inhibitory domain tagged with a nuclear localization signal. However, when pl 5 and p27 are forced to reside in the same subcellular location, either the cytoplasm or

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Genes & Development – Unpaywall

Published: Feb 15, 1997

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