CLASP2 interacts with p120-catenin and governs microtubule dynamics at adherens junctions

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CLASP2 interacts with p120-catenin and governs microtubule dynamics at adherens junctions. / Shahbazi, Marta N; Megias, Diego; Epifano, Carolina; Akhmanova, Anna; Gundersen, Gregg G; Fuchs, Elaine; Perez-Moreno, Mirna.

I: Journal of Cell Biology, Bind 203, Nr. 6, 2013, s. 1043-1061.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Shahbazi, MN, Megias, D, Epifano, C, Akhmanova, A, Gundersen, GG, Fuchs, E & Perez-Moreno, M 2013, 'CLASP2 interacts with p120-catenin and governs microtubule dynamics at adherens junctions', Journal of Cell Biology, bind 203, nr. 6, s. 1043-1061. https://doi.org/10.1083/jcb.201306019

APA

Shahbazi, M. N., Megias, D., Epifano, C., Akhmanova, A., Gundersen, G. G., Fuchs, E., & Perez-Moreno, M. (2013). CLASP2 interacts with p120-catenin and governs microtubule dynamics at adherens junctions. Journal of Cell Biology, 203(6), 1043-1061. https://doi.org/10.1083/jcb.201306019

Vancouver

Shahbazi MN, Megias D, Epifano C, Akhmanova A, Gundersen GG, Fuchs E o.a. CLASP2 interacts with p120-catenin and governs microtubule dynamics at adherens junctions. Journal of Cell Biology. 2013;203(6):1043-1061. https://doi.org/10.1083/jcb.201306019

Author

Shahbazi, Marta N ; Megias, Diego ; Epifano, Carolina ; Akhmanova, Anna ; Gundersen, Gregg G ; Fuchs, Elaine ; Perez-Moreno, Mirna. / CLASP2 interacts with p120-catenin and governs microtubule dynamics at adherens junctions. I: Journal of Cell Biology. 2013 ; Bind 203, Nr. 6. s. 1043-1061.

Bibtex

@article{b6385d1bf19e4ace883e92df226fe1f9,
title = "CLASP2 interacts with p120-catenin and governs microtubule dynamics at adherens junctions",
abstract = "Classical cadherins and their connections with microtubules (MTs) are emerging as important determinants of cell adhesion. However, the functional relevance of such interactions and the molecular players that contribute to tissue architecture are still emerging. In this paper, we report that the MT plus end-binding protein CLASP2 localizes to adherens junctions (AJs) via direct interaction with p120-catenin (p120) in primary basal mouse keratinocytes. Reductions in the levels of p120 or CLASP2 decreased the localization of the other protein to cell-cell contacts and altered AJ dynamics and stability. These features were accompanied by decreased MT density and altered MT dynamics at intercellular junction sites. Interestingly, CLASP2 was enriched at the cortex of basal progenitor keratinocytes, in close localization to p120. Our findings suggest the existence of a new mechanism of MT targeting to AJs with potential functional implications in the maintenance of proper cell-cell adhesion in epidermal stem cells.",
keywords = "Adherens Junctions, Animals, Catenins, Cell Adhesion, HEK293 Cells, Humans, Keratinocytes, Mice, Microtubule-Associated Proteins, Microtubules, Models, Biological, Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't",
author = "Shahbazi, {Marta N} and Diego Megias and Carolina Epifano and Anna Akhmanova and Gundersen, {Gregg G} and Elaine Fuchs and Mirna Perez-Moreno",
year = "2013",
doi = "10.1083/jcb.201306019",
language = "English",
volume = "203",
pages = "1043--1061",
journal = "Journal of Cell Biology",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "6",

}

RIS

TY - JOUR

T1 - CLASP2 interacts with p120-catenin and governs microtubule dynamics at adherens junctions

AU - Shahbazi, Marta N

AU - Megias, Diego

AU - Epifano, Carolina

AU - Akhmanova, Anna

AU - Gundersen, Gregg G

AU - Fuchs, Elaine

AU - Perez-Moreno, Mirna

PY - 2013

Y1 - 2013

N2 - Classical cadherins and their connections with microtubules (MTs) are emerging as important determinants of cell adhesion. However, the functional relevance of such interactions and the molecular players that contribute to tissue architecture are still emerging. In this paper, we report that the MT plus end-binding protein CLASP2 localizes to adherens junctions (AJs) via direct interaction with p120-catenin (p120) in primary basal mouse keratinocytes. Reductions in the levels of p120 or CLASP2 decreased the localization of the other protein to cell-cell contacts and altered AJ dynamics and stability. These features were accompanied by decreased MT density and altered MT dynamics at intercellular junction sites. Interestingly, CLASP2 was enriched at the cortex of basal progenitor keratinocytes, in close localization to p120. Our findings suggest the existence of a new mechanism of MT targeting to AJs with potential functional implications in the maintenance of proper cell-cell adhesion in epidermal stem cells.

AB - Classical cadherins and their connections with microtubules (MTs) are emerging as important determinants of cell adhesion. However, the functional relevance of such interactions and the molecular players that contribute to tissue architecture are still emerging. In this paper, we report that the MT plus end-binding protein CLASP2 localizes to adherens junctions (AJs) via direct interaction with p120-catenin (p120) in primary basal mouse keratinocytes. Reductions in the levels of p120 or CLASP2 decreased the localization of the other protein to cell-cell contacts and altered AJ dynamics and stability. These features were accompanied by decreased MT density and altered MT dynamics at intercellular junction sites. Interestingly, CLASP2 was enriched at the cortex of basal progenitor keratinocytes, in close localization to p120. Our findings suggest the existence of a new mechanism of MT targeting to AJs with potential functional implications in the maintenance of proper cell-cell adhesion in epidermal stem cells.

KW - Adherens Junctions

KW - Animals

KW - Catenins

KW - Cell Adhesion

KW - HEK293 Cells

KW - Humans

KW - Keratinocytes

KW - Mice

KW - Microtubule-Associated Proteins

KW - Microtubules

KW - Models, Biological

KW - Journal Article

KW - Research Support, N.I.H., Extramural

KW - Research Support, Non-U.S. Gov't

U2 - 10.1083/jcb.201306019

DO - 10.1083/jcb.201306019

M3 - Journal article

C2 - 24368809

VL - 203

SP - 1043

EP - 1061

JO - Journal of Cell Biology

JF - Journal of Cell Biology

SN - 0021-9525

IS - 6

ER -

ID: 188368550