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. Author manuscript; available in PMC: 2019 Mar 25.
Published in final edited form as: Matrix Biol. 2018 May 24;71-72:262–282. doi: 10.1016/j.matbio.2018.05.010

FIGURE 3. Syndecan-1 structure and binding to remnant lipoproteins.

FIGURE 3.

SDC1 is a type I transmembrane protein bearing up to three heparan sulfate and two chondroitin/dermatan sulfate chains. It undergoes homodimerization as well as proteolytic cleavage. The cleavage results in shedding of the large extracellular ectodomain bearing the HS chains. The short cytoplasmic tail contains the MKKK-endocytosis motif and interacts with a number of cytosolic proteins such as FLOT1 that play a role in clathrin- and caveolin-independent, raft-dependent endocytosis. A TRL containing ApoCIII is shown binding to the heparan sulfate chains via the interaction of sulfated domains with ApoE and ApoAV. GalNAc, N-acetylgalactosamine