Laminin-based cell adhesion anchors microtubule plus ends to the epithelial cell basal cortex through LL5 alpha/beta

A Hotta, T Kawakatsu, T Nakatani, T Sato, C Matsui, T Sukezane, T Akagi, T Hamaji, I Grigoriev, Anna Akhmanova, Y Takai, Y Mimori-Kiyosue

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LL5 beta 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 LL5 beta and its homologue LL5 alpha (LL5s) colocalize with autocrine laminin-5 and its receptors, integrins alpha 3 beta 1 and alpha 6 beta 4, 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 alpha 3 at the basal cell cortex. Activation of integrin alpha 3 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.
Original languageUndefined/Unknown
Pages (from-to)901-917
Number of pages17
JournalJournal of Cell Biology
Issue number5
Publication statusPublished - 2010

Research programs

  • EMC MGC-02-13-02

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