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Key regulators of galectin-glycan interactions
#MMPMID27582340
Kamili NA
; Arthur CM
; Gerner-Smidt C
; Tafesse E
; Blenda A
; Dias-Baruffi M
; Stowell SR
Proteomics
2016[Dec]; 16
(24
): 3111-3125
PMID27582340
show ga
Protein-ligand interactions serve as fundamental regulators of numerous
biological processes. Among protein-ligand pairs, glycan binding proteins (GBPs)
and the glycans they recognize represent unique and highly complex interactions
implicated in a broad range of regulatory activities. With few exceptions, cell
surface receptors and secreted proteins are heavily glycosylated. As these
glycans often represent highly regulatable post-translational modifications,
alterations in glycosylation can fundamentally impact GBP recognition. Among
GBPs, galectins in particular appear to engage a diverse set of glycan
determinants to impact a broad range of biological processes. In this review, we
will explore factors that impact galectin activity, including the effect of
glycan modification on galectin-glycan interactions.
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