UMMS Affiliation

Howard Hughes Medical Institute, Program in Molecular Medicine

Date

3-16-2005

Document Type

Article

Subjects

Adaptor Proteins, Signal Transducing; Animals; Cells, Cultured; Cercopithecus aethiops; Cloning, Molecular; Cytoplasm; Enzyme Activation; JNK Mitogen-Activated Protein Kinases; MAP Kinase Kinase 3; MAP Kinase Kinase 6; MAP Kinase Kinase 7; MAP Kinase Kinase Kinases; *MAP Kinase Signaling System; Mice; Mice, Knockout; Microtubule-Associated Proteins; Nerve Tissue Proteins; Phosphorylation; Protein Binding; p38 Mitogen-Activated Protein Kinases

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

The c-Jun NH2-terminal kinase (JNK)-interacting protein (JIP) group of scaffold proteins (JIP1, JIP2, and JIP3) can interact with components of the JNK signaling pathway and potently activate JNK. Here we describe the identification of a fourth member of the JIP family. The primary sequence of JIP4 is most closely related to that of JIP3. Like other members of the JIP family of scaffold proteins, JIP4 binds JNK and also the light chain of the microtubule motor protein kinesin-1. However, the function of JIP4 appears to be markedly different from other JIP proteins. Specifically, JIP4 does not activate JNK signaling. In contrast, JIP4 serves as an activator of the p38 mitogen-activated protein (MAP) kinase pathway by a mechanism that requires the MAP kinase kinases MKK3 and MKK6. The JIP4 scaffold protein therefore appears to be a new component of the p38 MAP kinase signaling pathway.

Rights and Permissions

Citation: Mol Cell Biol. 2005 Apr;25(7):2733-43. Link to article on publisher's site

DOI of Published Version

10.1128/MCB.25.7.2733-2743.2005

Related Resources

Link to Article in PubMed

Journal Title

Molecular and cellular biology

PubMed ID

15767678

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