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The interaction of Kinesin-1 with its adaptor protein JIP1 can be regulated via proteins binding to the JIP1-PTB domain

BACKGROUND: The regulatory mechanisms of motor protein-dependent intracellular transport are still not fully understood. The kinesin-1-binding protein, JIP1, can function as an adaptor protein that links kinesin-1 and other JIP1-binding “cargo” proteins. However, it is unknown whether these “cargo”...

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Autores principales: Satake, Tomoko, Otsuki, Karin, Banba, Yumi, Suenaga, Jun, Hirano, Hisashi, Yamanaka, Yuko, Ohno, Shigeo, Hirai, Syu-ichi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3599065/
https://www.ncbi.nlm.nih.gov/pubmed/23496950
http://dx.doi.org/10.1186/1471-2121-14-12
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author Satake, Tomoko
Otsuki, Karin
Banba, Yumi
Suenaga, Jun
Hirano, Hisashi
Yamanaka, Yuko
Ohno, Shigeo
Hirai, Syu-ichi
author_facet Satake, Tomoko
Otsuki, Karin
Banba, Yumi
Suenaga, Jun
Hirano, Hisashi
Yamanaka, Yuko
Ohno, Shigeo
Hirai, Syu-ichi
author_sort Satake, Tomoko
collection PubMed
description BACKGROUND: The regulatory mechanisms of motor protein-dependent intracellular transport are still not fully understood. The kinesin-1-binding protein, JIP1, can function as an adaptor protein that links kinesin-1 and other JIP1-binding “cargo” proteins. However, it is unknown whether these “cargo” proteins influence the JIP1–kinesin-1 binding. RESULTS: We show here that JIP1–kinesin-1 binding in Neuro2a cells was dependent on conserved amino acid residues in the JIP1-phosphotyrosine binding (PTB) domain, including F687. In addition, mutation of F687 severely affected the neurite tip localization of JIP1. Proteomic analysis revealed another kinesin-1 binding protein, JIP3, as a major JIP1 binding protein. The association between JIP1 and JIP3 was dependent on the F687 residue in JIP1, and this association induced the formation of a stable ternary complex with kinesin-1. On the other hand, the binding of JIP1 and JIP3 was independent of kinesin-1 binding. We also show that other PTB binding proteins can interrupt the formation of the ternary complex. CONCLUSIONS: The formation of the JIP1–kinesin-1 complex depends on the protein binding-status of the JIP1 PTB domain. This may imply a regulatory mechanism of kinesin-1-dependent intracellular transport.
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spelling pubmed-35990652013-03-17 The interaction of Kinesin-1 with its adaptor protein JIP1 can be regulated via proteins binding to the JIP1-PTB domain Satake, Tomoko Otsuki, Karin Banba, Yumi Suenaga, Jun Hirano, Hisashi Yamanaka, Yuko Ohno, Shigeo Hirai, Syu-ichi BMC Cell Biol Research Article BACKGROUND: The regulatory mechanisms of motor protein-dependent intracellular transport are still not fully understood. The kinesin-1-binding protein, JIP1, can function as an adaptor protein that links kinesin-1 and other JIP1-binding “cargo” proteins. However, it is unknown whether these “cargo” proteins influence the JIP1–kinesin-1 binding. RESULTS: We show here that JIP1–kinesin-1 binding in Neuro2a cells was dependent on conserved amino acid residues in the JIP1-phosphotyrosine binding (PTB) domain, including F687. In addition, mutation of F687 severely affected the neurite tip localization of JIP1. Proteomic analysis revealed another kinesin-1 binding protein, JIP3, as a major JIP1 binding protein. The association between JIP1 and JIP3 was dependent on the F687 residue in JIP1, and this association induced the formation of a stable ternary complex with kinesin-1. On the other hand, the binding of JIP1 and JIP3 was independent of kinesin-1 binding. We also show that other PTB binding proteins can interrupt the formation of the ternary complex. CONCLUSIONS: The formation of the JIP1–kinesin-1 complex depends on the protein binding-status of the JIP1 PTB domain. This may imply a regulatory mechanism of kinesin-1-dependent intracellular transport. BioMed Central 2013-03-04 /pmc/articles/PMC3599065/ /pubmed/23496950 http://dx.doi.org/10.1186/1471-2121-14-12 Text en Copyright ©2013 Satake et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Satake, Tomoko
Otsuki, Karin
Banba, Yumi
Suenaga, Jun
Hirano, Hisashi
Yamanaka, Yuko
Ohno, Shigeo
Hirai, Syu-ichi
The interaction of Kinesin-1 with its adaptor protein JIP1 can be regulated via proteins binding to the JIP1-PTB domain
title The interaction of Kinesin-1 with its adaptor protein JIP1 can be regulated via proteins binding to the JIP1-PTB domain
title_full The interaction of Kinesin-1 with its adaptor protein JIP1 can be regulated via proteins binding to the JIP1-PTB domain
title_fullStr The interaction of Kinesin-1 with its adaptor protein JIP1 can be regulated via proteins binding to the JIP1-PTB domain
title_full_unstemmed The interaction of Kinesin-1 with its adaptor protein JIP1 can be regulated via proteins binding to the JIP1-PTB domain
title_short The interaction of Kinesin-1 with its adaptor protein JIP1 can be regulated via proteins binding to the JIP1-PTB domain
title_sort interaction of kinesin-1 with its adaptor protein jip1 can be regulated via proteins binding to the jip1-ptb domain
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3599065/
https://www.ncbi.nlm.nih.gov/pubmed/23496950
http://dx.doi.org/10.1186/1471-2121-14-12
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