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Laminin-based cell adhesion anchors microtubule plus ends to the epithelial cell basal cortex through LL5α/β

LL5β has been identified as a microtubule-anchoring factor that attaches EB1/CLIP-associating protein (CLASP)–bound microtubule plus ends to the cell cortex. In this study, we show that LL5β and its homologue LL5α (LL5s) colocalize with autocrine laminin-5 and its receptors, integrins α3β1 and α6β4,...

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Autores principales: Hotta, Azusa, Kawakatsu, Tomomi, Nakatani, Tomoya, Sato, Toshitaka, Matsui, Chiyuki, Sukezane, Taiko, Akagi, Tsuyoshi, Hamaji, Tomoko, Grigoriev, Ilya, Akhmanova, Anna, Takai, Yoshimi, Mimori-Kiyosue, Yuko
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2878951/
https://www.ncbi.nlm.nih.gov/pubmed/20513769
http://dx.doi.org/10.1083/jcb.200910095
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author Hotta, Azusa
Kawakatsu, Tomomi
Nakatani, Tomoya
Sato, Toshitaka
Matsui, Chiyuki
Sukezane, Taiko
Akagi, Tsuyoshi
Hamaji, Tomoko
Grigoriev, Ilya
Akhmanova, Anna
Takai, Yoshimi
Mimori-Kiyosue, Yuko
author_facet Hotta, Azusa
Kawakatsu, Tomomi
Nakatani, Tomoya
Sato, Toshitaka
Matsui, Chiyuki
Sukezane, Taiko
Akagi, Tsuyoshi
Hamaji, Tomoko
Grigoriev, Ilya
Akhmanova, Anna
Takai, Yoshimi
Mimori-Kiyosue, Yuko
author_sort Hotta, Azusa
collection PubMed
description LL5β has been identified as a microtubule-anchoring factor that attaches EB1/CLIP-associating protein (CLASP)–bound microtubule plus ends to the cell cortex. In this study, we show that LL5β and its homologue LL5α (LL5s) colocalize with autocrine laminin-5 and its receptors, integrins α3β1 and α6β4, at the basal side of fully polarized epithelial sheets. Depletion of both laminin receptor integrins abolishes the cortical localization of LL5s, whereas LL5 depletion reduces the amount of integrin α3 at the basal cell cortex. Activation of integrin α3 is sufficient to initiate LL5 accumulation at the cell cortex. LL5s form a complex with the cytoplasmic tails of these integrins, but their interaction might be indirect. Analysis of the three-dimensional distribution of microtubule growth by visualizing EB1-GFP in epithelial sheets in combination with RNA interference reveals that LL5s are required to maintain the density of growing microtubules selectively at the basal cortex. These findings reveal that signaling from laminin–integrin associations attaches microtubule plus ends to the epithelial basal cell cortex.
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spelling pubmed-28789512010-11-30 Laminin-based cell adhesion anchors microtubule plus ends to the epithelial cell basal cortex through LL5α/β Hotta, Azusa Kawakatsu, Tomomi Nakatani, Tomoya Sato, Toshitaka Matsui, Chiyuki Sukezane, Taiko Akagi, Tsuyoshi Hamaji, Tomoko Grigoriev, Ilya Akhmanova, Anna Takai, Yoshimi Mimori-Kiyosue, Yuko J Cell Biol Research Articles LL5β has been identified as a microtubule-anchoring factor that attaches EB1/CLIP-associating protein (CLASP)–bound microtubule plus ends to the cell cortex. In this study, we show that LL5β and its homologue LL5α (LL5s) colocalize with autocrine laminin-5 and its receptors, integrins α3β1 and α6β4, at the basal side of fully polarized epithelial sheets. Depletion of both laminin receptor integrins abolishes the cortical localization of LL5s, whereas LL5 depletion reduces the amount of integrin α3 at the basal cell cortex. Activation of integrin α3 is sufficient to initiate LL5 accumulation at the cell cortex. LL5s form a complex with the cytoplasmic tails of these integrins, but their interaction might be indirect. Analysis of the three-dimensional distribution of microtubule growth by visualizing EB1-GFP in epithelial sheets in combination with RNA interference reveals that LL5s are required to maintain the density of growing microtubules selectively at the basal cortex. These findings reveal that signaling from laminin–integrin associations attaches microtubule plus ends to the epithelial basal cell cortex. The Rockefeller University Press 2010-05-31 /pmc/articles/PMC2878951/ /pubmed/20513769 http://dx.doi.org/10.1083/jcb.200910095 Text en © 2010 Hotta et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).
spellingShingle Research Articles
Hotta, Azusa
Kawakatsu, Tomomi
Nakatani, Tomoya
Sato, Toshitaka
Matsui, Chiyuki
Sukezane, Taiko
Akagi, Tsuyoshi
Hamaji, Tomoko
Grigoriev, Ilya
Akhmanova, Anna
Takai, Yoshimi
Mimori-Kiyosue, Yuko
Laminin-based cell adhesion anchors microtubule plus ends to the epithelial cell basal cortex through LL5α/β
title Laminin-based cell adhesion anchors microtubule plus ends to the epithelial cell basal cortex through LL5α/β
title_full Laminin-based cell adhesion anchors microtubule plus ends to the epithelial cell basal cortex through LL5α/β
title_fullStr Laminin-based cell adhesion anchors microtubule plus ends to the epithelial cell basal cortex through LL5α/β
title_full_unstemmed Laminin-based cell adhesion anchors microtubule plus ends to the epithelial cell basal cortex through LL5α/β
title_short Laminin-based cell adhesion anchors microtubule plus ends to the epithelial cell basal cortex through LL5α/β
title_sort laminin-based cell adhesion anchors microtubule plus ends to the epithelial cell basal cortex through ll5α/β
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2878951/
https://www.ncbi.nlm.nih.gov/pubmed/20513769
http://dx.doi.org/10.1083/jcb.200910095
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