Small GTPase Rab21 regulates cell adhesion and controls endosomal traffic of β1-integrins

Teijo Pellinen, Antti Arjonen, Karoliina Vuoriluoto, Katja Kallio, Jack A. M. Fransen, Johanna Ivaska

Research output: Contribution to journalArticleScientificpeer-review

275 Citations (Scopus)


Dynamic turnover of integrin cell adhesion molecules to and from the cell surface is central to cell migration. We report for the first time an association between integrins and Rab proteins, which are small GTPases involved in the traffic of endocytotic vesicles. Rab21 (and Rab5) associate with the cytoplasmic domains of α-integrin chains, and their expression influences the endo/exocytic traffic of integrins. This function of Rab21 is dependent on its GTP/GDP cycle and proper membrane targeting. Knock down of Rab21 impairs integrin-mediated cell adhesion and motility, whereas its overexpression stimulates cell migration and cancer cell adhesion to collagen and human bone. Finally, overexpression of Rab21 fails to induce cell adhesion via an integrin point mutant deficient in Rab21 association. These data provide mechanistic insight into how integrins are targeted to intracellular compartments and how their traffic regulates cell adhesion.
Original languageEnglish
Pages (from-to)767-780
JournalJournal of Cell Biology
Issue number5
Publication statusPublished - 2006
MoE publication typeA1 Journal article-refereed


  • integrin
  • cell migration
  • Rab
  • GTPases
  • proteins


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