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Physiology

Western University

Theses/Dissertations

Integrin-linked kinase

Publication Year

Articles 1 - 4 of 4

Full-Text Articles in Life Sciences

Identification Of A Novel Interaction Between Integrin-Linked Kinase And Beta-Arrestin 1, Hannah E. Murphy-Marshman Sep 2016

Identification Of A Novel Interaction Between Integrin-Linked Kinase And Beta-Arrestin 1, Hannah E. Murphy-Marshman

Electronic Thesis and Dissertation Repository

Integrin-linked kinase (ILK) is a ubiquitous scaffold protein essential for the development of front-rear polarity and directional migration of epidermal keratinocytes. β-arrestin 1 is another adaptor protein which has recently emerged as a key factor in modulating proliferation and migration of various cell types. Previous studies have demonstrated an association between β-arrestin 2 and ILK in cerebellar granule precursor cells. I have now identified a novel interaction between ILK and β-arrestin 1 in primary keratinocytes that occurs directly and without post-translational modifications. The N-terminal 67 residues of ILK and multiple regions in β-arrestin 1 are important for this interaction. This …


A Rhog/Ilk/Elmo2/Rac1 Pathways Modulates Microtubule Stability, Bradley C. Jackson Sep 2014

A Rhog/Ilk/Elmo2/Rac1 Pathways Modulates Microtubule Stability, Bradley C. Jackson

Electronic Thesis and Dissertation Repository

Integrin-linked kinase (ILK) is a widely expressed scaffold protein important for cell adhesion, migration, and phagocytosis. ILK and its interacting partner, engulfment and cell motility protein 2 (ELMO2), may also modulate microtubule dynamics. Here, I show that sustained microtubule growth and acetylated tubulin levels are reduced in the absence of ILK and, conversely, that exogenous ILK exerts a stabilizing effect on microtubules. Further, exogenous ELMO2, ras homology growth related protein (RHOG) and ras-related C3 botulinum toxin substrate 1 (RAC1) stabilize microtubules in an ILK-dependent manner. Potential downstream effectors of the effect of ILK on microtubule stability include glycogen synthase kinase- …


Ilk Modulates Stress-Induced Apoptosis In Epidermal Keratinocytes, Michelle Im Aug 2014

Ilk Modulates Stress-Induced Apoptosis In Epidermal Keratinocytes, Michelle Im

Electronic Thesis and Dissertation Repository

Integrin-linked kinase (ILK) is a ubiquitous scaffold protein that mediates cellular responses to integrin stimulation by extracellular matrix proteins. Mice with inactivation of the Ilk gene in squamous epithelia display defects in skin regeneration after injury, failure to thrive, and perinatal death. ILK-deficient epidermis exhibits reduced adhesion to the basement membrane and impaired hair follicle morphogenesis. In culture, ILK-deficient keratinocytes fail to attach and spread efficiently, and demonstrate decreased survival. We now show that ILK-deficient keratinocytes exhibit lower proliferative capacity and increased apoptosis in the absence or presence of growth factors. This reduced viability appears to be independent of the …


Transforming Growth Factor-Beta Receptor Signalling Is Modulated By Integrin-Linked Kinase, Stellar H. Boo Nov 2013

Transforming Growth Factor-Beta Receptor Signalling Is Modulated By Integrin-Linked Kinase, Stellar H. Boo

Electronic Thesis and Dissertation Repository

Transforming growth factor-beta 1 (TGF-β1) modulates regeneration after injury through induction of fibroblast proliferation, migration, and differentiation into myofibroblasts. Induction of myofibroblast differentiation by TGF-β1 requires expression of integrin-linked kinase (ILK). I now show that ILK interacts with TGF-β receptor type II (TβRII) in primary dermal fibroblasts. Further, colocalization of ILK and TβRII can be observed at the cell membrane and in intracellular vesicles. The association of TβRII and ILK does not require TGF-β1 stimulation, kinase activity of TGF-β1 receptor type I or TβRII, and it does not involve interactions between ILK and focal adhesion-associated proteins. When this interaction is …