Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation.

By K. Lau, E. Partridge, A. Grigorian, Cristina I. Silvescu, V. Reinhold, M. Demetriou, J. Dennis. Cell, 2007

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Protein-glycan interactions in the control of innate and adaptive immune responses (2008, background): “The authors recently extended these findings showing that metabolite supply of the hexosamine pathway restores the high-affinity ligands for galectins, which suppresses TCR signaling and proliferation, inhibits T H 1 skewing and prevents the development of autoimmune inflammatio”
Turning 'sweet' on immunity: galectin–glycan interactions in immune tolerance and inflammation (2009, background): “This variable number of N-glycans can selectively regulate receptor turnover and endocytosi”
Biological roles of glycans (2016, background): “Thus, there are reports of regulation of cytokine receptors by modulation of endocytosis rates by the type of glycan structure and branching (605), and N-glycan number and degree of branching can cooperate to regulate cell proliferation and differentiation (606) as 10 A Varki”
Mammalian glycosylation in immunity (2008, neutral): “There is increasing evidence that mammalian glycosylation controls the rate of receptor endocytosis as a means to modulate cellular responses through the interaction of lectins and their ligand”