Variant glycosylation: an underappreciated regulatory mechanism for beta1 integrins.
Although it has been known for many years that beta1 integrins undergo differential glycosylation in accordance with changes in cell phenotype, the potential role of N-glycosylation as a modulator of integrin function has received little attention. One reason for the relatively limited interest in this topic likely relates to the fact that much of the prior research was correlative in nature. However, new results now bolster the hypothesis that there is a causal relationship between variant glycosylation and altered integrin activity. In this review, the evidence for variant glycosylation as a regulatory mechanism for beta1 integrins are summarized, with particular emphasis on: (1). outlining the instances in which cell phenotypic variation is associated with differential beta1 glycosylation, (2). describing the specific alterations in glycan structure that accompany phenotypic changes and (3). presenting potential mechanisms by which variant glycosylation might regulate integrin function.
Bellis
Susan L
SL
Department of Physiology and Biophysics, University of Alabama at Birmingham, MCLM 982A, 1918 University Boulevard, Birmingham, AL 35294, USA. bellis@physiology.uab.edu
D000818:Animals; D002454:Cell Differentiation; D002460:Cell Line; D006031:Glycosylation; D006801:Humans; D019012:Integrin beta1 / Q000378:metabolism* / Q000502:physiology; D009844:Oligosaccharides / Q000737:chemistry / Q000378:metabolism; D010641:Phenotype
D019012:Integrin beta1; D009844:Oligosaccharides