Question

(a) Glypican is a heparin sulfate proteoglycan attached to the plasma membrane by a GPI anchor. Nevertheless, glypicans are actively involved in several transmembrane signaling processes. Describe a hypothetical mechanism by which glypican could direct transmembrane signaling.

(b) Briefly, propose a general strategy for experimentally testing your proposed mechanism in part a.

Answer 1

Answer 1:)

Glypicans are heparan sulfate proteoglycans that are bound to the outside surface of the plasma layer by a glycosyl-phosphatidylinositol (GPI) linkage. Most glypicans, including those of Drosophila, are exposed to endoproteolytic cleavage by a furin-like convertase.

The following mechanism could be possible for the effect of glypicans on transmembrane signaling.

In vivo proof distributed so far shows that the principle capacity of layer joined glypicans is to manage the motioning of Wnts, Hedgehogs, fibroblast development factors, and bone morphogenetic proteins (BMPs). Because of Wnt, it has been suggested that the stimulatory system depends on the capacity of glypicans to encourage and additionally balance out the connection of Wnts with their flagging receptors, the Frizzled proteins. Then again, GPC3 is responsible for hindering Hedgehog protein motioning during improvement by contending with Patched, the Hedgehog receptor, for Hedgehog authoritative. Shockingly, the administrative action of glypicans in the Wnt, Hedgehog and BMP flagging pathways is just somewhat subject to the heparan sulfate chains. Contingent upon the above specific features, glypicans may have a stimulatory or inhibitory movement on transmembrane signaling.