The triple helix of collagens - an ancient protein structure that enabled animal multicellularity and tissue evolution.

Abstract:

:The cellular microenvironment, characterized by an extracellular matrix (ECM), played an essential role in the transition from unicellularity to multicellularity in animals (metazoans), and in the subsequent evolution of diverse animal tissues and organs. A major ECM component are members of the collagen superfamily -comprising 28 types in vertebrates - that exist in diverse supramolecular assemblies ranging from networks to fibrils. Each assembly is characterized by a hallmark feature, a protein structure called a triple helix. A current gap in knowledge is understanding the mechanisms of how the triple helix encodes and utilizes information in building scaffolds on the outside of cells. Type IV collagen, recently revealed as the evolutionarily most ancient member of the collagen superfamily, serves as an archetype for a fresh view of fundamental structural features of a triple helix that underlie the diversity of biological activities of collagens. In this Opinion, we argue that the triple helix is a protein structure of fundamental importance in building the extracellular matrix, which enabled animal multicellularity and tissue evolution.

journal_name

J Cell Sci

journal_title

Journal of cell science

authors

Fidler AL,Boudko SP,Rokas A,Hudson BG

doi

10.1242/jcs.203950

subject

Has Abstract

pub_date

2018-04-09 00:00:00

issue

7

eissn

0021-9533

issn

1477-9137

pii

131/7/jcs203950

journal_volume

131

pub_type

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