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JLP: A scaffolding protein that tethers JNK/p38MAPK signaling modules and transcription factors.

ABSTRACT: Extracellular signals are transduced into cells through mitogen-activated protein kinases (MAPKs), which are activated by their upstream kinases. Recently, families of scaffolding proteins have been identified to tether specific combinations of these kinases along specific signaling pathways. Here we describe a protein, JLP (c-Jun NH2-terminal kinase-associated leucine zipper protein), which acts as a scaffolding protein to bring together Max and c-Myc along with JNK (c-Jun NH2-terminal kinase) and p38MAPK, as well as their upstream kinases MKK4 (MAPK kinase 4) and MEKK3 (MAPK kinase kinase 3). Thus, JLP defines a family of scaffolding proteins that bring MAPKs and their target transcription factors together for the execution of specific signaling pathways.

SUBMITTER: Lee CM

PROVIDER: S-EPMC137859 | biostudies-literature | 2002 Oct

REPOSITORIES: biostudies-literature

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JLP: A scaffolding protein that tethers JNK/p38MAPK signaling modules and transcription factors.

Lee Clement M CM Onésime Djamila D Reddy C Damodara CD Dhanasekaran N N Reddy E Premkumar EP

Proceedings of the National Academy of Sciences of the United States of America 20021021 22

Extracellular signals are transduced into cells through mitogen-activated protein kinases (MAPKs), which are activated by their upstream kinases. Recently, families of scaffolding proteins have been identified to tether specific combinations of these kinases along specific signaling pathways. Here we describe a protein, JLP (c-Jun NH2-terminal kinase-associated leucine zipper protein), which acts as a scaffolding protein to bring together Max and c-Myc along with JNK (c-Jun NH2-terminal kinase) ...[more]

PMID: 12391307

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