English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

ILK: a pseudokinase with a unique function in the integrin-actin linkage

MPS-Authors

Ghatak,  S.
Max Planck Society;

Morgner,  J.
Max Planck Society;

Wickström,  S. A.
Max Planck Society;

Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)
There is no public supplementary material available
Citation

Ghatak, S., Morgner, J., & Wickström, S. A. (2013). ILK: a pseudokinase with a unique function in the integrin-actin linkage. Biochem Soc Trans, 41(4), 995-1001. doi:10.1042/BST20130062.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0028-58E6-7
Abstract
ILK (integrin-linked kinase) is a central component of cell-matrix adhesions and an important regulator of integrin function. It forms a ternary complex with two other adaptor proteins, PINCH (particularly interesting cysteine- and histidine-rich protein) and parvin, forming the IPP (ILK-PINCH-parvin) complex that regulates the integrin-actin linkage as well as microtubule dynamics. These functions are essential for processes such as cell migration and matrix remodelling. The present review discusses the recent advances on the structural and functional characterization of ILK and the long-standing debate regarding its reported kinase activity.