Disruption of the integrin-linked kinase (ILK) pseudokinase domain affects kidney development in mice

Nada Bulus,Kyle L Brown,Glenda Mernaugh,Anika Böttcher,Xinyu Dong,Charles R Sanders,Ambra Pozzi,Reinhard Fässler,Roy Zent

doi:10.1016/j.jbc.2021.100361

Abstract

Disruption of the integrin-linked kinase (ILK) pseudokinase domain affects kidney development in mice

Highlights

Pseudokinase protein consisting of an N-terminal domain with five ankyrin repeats, a COOH-terminal pseudo kinase domain, and an intervening pleckstrin homology (PH) domain [1,2,3,4]
We previously showed that deleting Integrin-linked kinase (ILK) in the developing ureteric bud (UB) of the kidney results in a branching morphogenesis defect and that ILK-null collecting duct (CD) cells have abnormalities in multiple integrin-dependent functions [7]
The paxillin-binding site (PBS) and K220M mutant mice were born in the correct Mendelian ratio while the E359K mutants were born at a lower ratio (6.7%), which was similar to the mice lacking ILK in the UB (8.1%), suggesting that some of these mice died in utero or at birth

Summary

Introduction

Pseudokinase protein consisting of an N-terminal domain with five ankyrin repeats, a COOH-terminal pseudo kinase domain, and an intervening pleckstrin homology (PH) domain [1,2,3,4]. Immunoblots of total cell lysates of CD cells expressing WTILK and the K220M mutation demonstrated that all three components of the IPP complex as well as paxillin were present (Fig. 3, A and B); similar to cells lacking ILK (KO), there was almost no α-parvin in the lysates of the E359K and PBS mutants (Fig. 3, A and B). There were no differences in the amount of pinch or paxillin in cells expressing WT-ILK or any of the mutants (Fig. 3, A and B).

Results

Conclusion