PUBLICATION

A mechanism of Rap1-induced stabilization of endothelial cell--cell junctions

Authors
Liu, J.J., Stockton, R.A., Gingras, A.R., Ablooglu, A.J., Han, J., Bobkov, A.A., Ginsberg, M.H.
ID
ZDB-PUB-190719-5
Date
2011
Source
Molecular biology of the cell   22: 2509-19 (Journal)
Registered Authors
Ablooglu, Ararat
Keywords
none
MeSH Terms
  • Animals
  • Cardiovascular System/growth & development
  • Cardiovascular System/metabolism
  • Endothelial Cells/metabolism
  • Endothelial Cells/physiology
  • Gene Expression
  • Genetic Vectors
  • HEK293 Cells
  • Humans
  • Intercellular Junctions/genetics*
  • Intercellular Junctions/metabolism
  • KRIT1 Protein
  • Microtubule-Associated Proteins/chemistry
  • Microtubule-Associated Proteins/genetics
  • Microtubule-Associated Proteins/metabolism*
  • Microtubules/genetics
  • Microtubules/metabolism
  • Monomeric GTP-Binding Proteins/chemistry
  • Monomeric GTP-Binding Proteins/genetics
  • Monomeric GTP-Binding Proteins/metabolism*
  • Muscle Proteins/genetics
  • Muscle Proteins/metabolism*
  • Muscle Proteins/physiology
  • Protein Conformation
  • Protein Structure, Tertiary
  • Proto-Oncogene Proteins/chemistry
  • Proto-Oncogene Proteins/genetics
  • Proto-Oncogene Proteins/metabolism*
  • RNA, Small Interfering
  • Signal Transduction
  • Structure-Activity Relationship
  • Umbilical Veins/cytology
  • Zebrafish/genetics
  • Zebrafish/growth & development*
  • Zebrafish/metabolism
  • Zebrafish Proteins/chemistry
  • Zebrafish Proteins/genetics
  • Zebrafish Proteins/metabolism*
  • Zebrafish Proteins/physiology
  • rap1 GTP-Binding Proteins/chemistry
  • rap1 GTP-Binding Proteins/genetics
  • rap1 GTP-Binding Proteins/metabolism*
PubMed
21633110 Full text @ Mol. Biol. Cell
Abstract
Activation of Rap1 small GTPases stabilizes cell--cell junctions, and this activity requires Krev Interaction Trapped gene 1 (KRIT1). Loss of KRIT1 disrupts cardiovascular development and causes autosomal dominant familial cerebral cavernous malformations. Here we report that native KRIT1 protein binds the effector loop of Rap1A but not H-Ras in a GTP-dependent manner, establishing that it is an authentic Rap1-specific effector. By modeling the KRIT1-Rap1 interface we designed a well-folded KRIT1 mutant that exhibited a ~40-fold-reduced affinity for Rap1A and maintained other KRIT1-binding functions. Direct binding of KRIT1 to Rap1 stabilized endothelial cell-cell junctions in vitro and was required for cardiovascular development in vivo. Mechanistically, Rap1 binding released KRIT1 from microtubules, enabling it to locate to cell--cell junctions, where it suppressed Rho kinase signaling and stabilized the junctions. These studies establish that the direct physical interaction of Rap1 with KRIT1 enables the translocation of microtubule-sequestered KRIT1 to junctions, thereby supporting junctional integrity and cardiovascular development.
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