Intracellular nanovesicles mediate α5β1 integrin trafficking during cell migration.

Autor:	Larocque G; Centre for Mechanochemical Cell Biology, Warwick Medical School, Coventry, UK., Moore DJ; Centre for Mechanochemical Cell Biology, Warwick Medical School, Coventry, UK., Sittewelle M; Centre for Mechanochemical Cell Biology, Warwick Medical School, Coventry, UK., Kuey C; Centre for Mechanochemical Cell Biology, Warwick Medical School, Coventry, UK., Hetmanski JHR; Wellcome Trust Centre for Cell-Matrix Research, Faculty of Biology, Medicine and Health, University of Manchester, Manchester Academic Health Science Centre, Manchester, UK., La-Borde PJ; Centre for Mechanochemical Cell Biology, Warwick Medical School, Coventry, UK., Wilson BJ; Wellcome Trust Centre for Cell-Matrix Research, Faculty of Biology, Medicine and Health, University of Manchester, Manchester Academic Health Science Centre, Manchester, UK., Clarke NI; Centre for Mechanochemical Cell Biology, Warwick Medical School, Coventry, UK., Caswell PT; Wellcome Trust Centre for Cell-Matrix Research, Faculty of Biology, Medicine and Health, University of Manchester, Manchester Academic Health Science Centre, Manchester, UK., Royle SJ; Centre for Mechanochemical Cell Biology, Warwick Medical School, Coventry, UK.
Jazyk:	angličtina
Zdroj:	The Journal of cell biology [J Cell Biol] 2021 Oct 04; Vol. 220 (10). Date of Electronic Publication: 2021 Jul 21.
DOI:	10.1083/jcb.202009028
Abstrakt:	Membrane traffic is an important regulator of cell migration through the endocytosis and recycling of cell surface receptors such as integrin heterodimers. Intracellular nanovesicles (INVs) are transport vesicles that are involved in multiple membrane trafficking steps, including the recycling pathway. The only known marker for INVs is tumor protein D54 (TPD54/TPD52L2), a member of the TPD52-like protein family. Overexpression of TPD52-like family proteins in cancer has been linked to poor prognosis and an aggressive metastatic phenotype, which suggests cell migration may be altered under these conditions. Here, we show that TPD54 directly binds membrane and associates with INVs via a conserved positively charged motif in its C terminus. We describe how other TPD52-like proteins are also associated with INVs, and we document the Rab GTPase complement of all INVs. Depletion of TPD52-like proteins inhibits cell migration and invasion, while their overexpression boosts motility. We show that inhibition of migration is likely due to altered recycling of α5β1 integrins in INVs. (© 2021 Larocque et al.)
Databáze:	MEDLINE
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