• English
    • Norsk
  • English 
    • English
    • Norsk
  • Administration
View Item 
  •   Home
  • Øvrige samlinger
  • Høstingsarkiver
  • CRIStin høstingsarkiv
  • View Item
  •   Home
  • Øvrige samlinger
  • Høstingsarkiver
  • CRIStin høstingsarkiv
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

Rab6 regulates cell migration and invasion by recruiting Cdc42 and modulating its activity.

Vestre, Katharina; Kjos, Ingrid; Guadagno, Noemi Antonella; Distefano, Marita Borg; Kohler, Felix; Fenaroli, Federico; Bakke, Oddmund; Progida, Cinzia
Journal article; AcceptedVersion; Peer reviewed
View/Open
Vestre%2C+Kjos+et+al+2019.pdf (3.815Mb)
Year
2019
Permanent link
http://urn.nb.no/URN:NBN:no-78088

CRIStin
1755602

Metadata
Show metadata
Appears in the following Collection
  • Institutt for biovitenskap [1177]
  • Institutt for klinisk medisin [5366]
  • Det matematisk-naturvitenskapelige fakultet [251]
  • CRIStin høstingsarkiv [15189]
Original version
Cellular and Molecular Life Sciences (CMLS). 2019, 76 (13), 2593-2614, DOI: https://doi.org/10.1007/s00018-019-03057-w
Abstract
Rab proteins are master regulators of intracellular membrane trafficking, but they also contribute to cell division, signaling, polarization, and migration. The majority of the works describing the mechanisms used by Rab proteins to regulate cell motility involve intracellular transport of key molecules important for migration. Interestingly, a few studies indicate that Rabs can modulate the activity of Rho GTPases, important regulators for the cytoskeleton rearrangements, but the mechanisms behind this crosstalk are still poorly understood. In this work, we identify Rab6 as a negative regulator of cell migration in vitro and in vivo. We show that the loss of Rab6 promotes formation of actin protrusions and influences actomyosin dynamics by upregulating Cdc42 activity and downregulating myosin II phosphorylation. We further provide the molecular mechanism behind this regulation demonstrating that Rab6 interacts with both Cdc42 and Trio, a GEF for Cdc42. In sum, our results uncover a mechanism used by Rab proteins to ensure spatial regulation of Rho GTPase activity for coordination of cytoskeleton rearrangements required in migrating cells.
 
Responsible for this website 
University of Oslo Library


Contact Us 
duo-hjelp@ub.uio.no


Privacy policy
 

 

For students / employeesSubmit master thesisAccess to restricted material

Browse

All of DUOCommunities & CollectionsBy Issue DateAuthorsTitlesThis CollectionBy Issue DateAuthorsTitles

For library staff

Login
RSS Feeds
 
Responsible for this website 
University of Oslo Library


Contact Us 
duo-hjelp@ub.uio.no


Privacy policy