TY - JOUR

T1 - Comparative characteristics of the structure and function for animal syndecan-1 proteins

AU - Leonova, E. I.

AU - Galzitskaya, O. V.

PY - 2013/5/1

Y1 - 2013/5/1

N2 - Syndecan-1 is a major transmembrane proteoglycan and performs diverse functions in multicellular organisms, affecting the cell interactions, acting as a coreceptor to bind with many ligands and to integrate them with their receptors, playing a protective role, and influencing regeneration and tumorigenesis. Syndecan-1, as well as the total extracellular matrix, plays an important developmental role. The functional diversity is related with the syndecan-1 structure. The extracellular and cytoplasmic domains of syndecan-1 were found to be intrinsically disordered. This feature allows syndecan-1 to to bind with adapter proteins in the cytoplasm and be extended with glycosaminoglycans in the extracellular matrix, and to take part in the diverse and important cellular processes. The occurrences of 20 amino acids in syndecan-1 proteins from 32 animals were compared with those in 17 animal proteomes. Gly, Thr, Gln, Glu, and Pro were found to predominate in the former, facilitating the lack of an ordered structure.

AB - Syndecan-1 is a major transmembrane proteoglycan and performs diverse functions in multicellular organisms, affecting the cell interactions, acting as a coreceptor to bind with many ligands and to integrate them with their receptors, playing a protective role, and influencing regeneration and tumorigenesis. Syndecan-1, as well as the total extracellular matrix, plays an important developmental role. The functional diversity is related with the syndecan-1 structure. The extracellular and cytoplasmic domains of syndecan-1 were found to be intrinsically disordered. This feature allows syndecan-1 to to bind with adapter proteins in the cytoplasm and be extended with glycosaminoglycans in the extracellular matrix, and to take part in the diverse and important cellular processes. The occurrences of 20 amino acids in syndecan-1 proteins from 32 animals were compared with those in 17 animal proteomes. Gly, Thr, Gln, Glu, and Pro were found to predominate in the former, facilitating the lack of an ordered structure.

KW - disordered residues

KW - extracellular matrix

KW - heparan sulfate

KW - motifs with low complexity

KW - proteoglycan

KW - syndecan

UR - http://www.scopus.com/inward/record.url?scp=84879188336&partnerID=8YFLogxK

U2 - 10.1134/S0026893313030060

DO - 10.1134/S0026893313030060

M3 - Article

AN - SCOPUS:84879188336

VL - 47

SP - 446

EP - 452

JO - Molecular Biology

JF - Molecular Biology

SN - 0026-8933

IS - 3

ER -