Related Experiment Video
Updated: Jul 2, 2026

A Functional Assay for Gap Junctional Examination; Electroporation of Adherent Cells on Indium-Tin Oxide
Published on: October 18, 2014
SHIP2 associates with intersectin and recruits it to the plasma membrane in response to EGF
Jingwei Xie1, Isabelle Vandenbroere, Isabelle Pirson
1Institute of Interdisciplinary Research, Free University of Brussels, Route de Lennik 808, B-1070 Brussels, Belgium.
Abstract:
We identified intersectin1 (ITSN1) as a new binding partner of the SH2 domain containing inositol 5-phosphatase 2 (SHIP2). The interaction between SHIP2 and ITSN1 was confirmed in vivo. Src homology 3D, A, C, and E domains of ITSN1 were shown to be implicated in the interaction. In response to epidermal growth factor, SHIP2 expression could recruit the ITSN1 short form (ITSN1-S) to the cell membrane, while SHIP2 overexpression did not modulate the ITSN-mediated extracellular signal-regulated kinase1/2 and c-Jun NH2-terminal kinase activation. Our data provide a molecular link between SHIP2 and ITSN1 which are involved in receptor endocytosis regulation.
More Related Videos
Related Concept Videos
Intracellular Signaling Affects Focal Adhesions
Some...
Anchoring Junctions
Overview of Cell-Matrix Interactions
Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal
Assembly of Signaling Complexes
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
GPI Anchoring of Proteins in the ER Membrane
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...

