Collagen fibril assembly: New approaches to unanswered questions

Christopher K. Revell, Oliver E. Jensen, Tom Shearer, Yinhui Lu, David F. Holmes, Karl E. Kadler

Research output: Contribution to journalArticlepeer-review

Abstract

Collagen fibrils are essential for metazoan life. They are the largest, most abundant, and most versatile protein polymers in animals, where they occur in the extracellular matrix to form the structural basis of tissues and organs. Collagen fibrils were first observed at the turn of the 20th century. During the last 40 years, the genes that encode the family of collagens have been identified, the structure of the collagen triple helix has been solved, the many enzymes involved in the post-translational modifications of collagens have been identified, mutations in the genes encoding collagen and collagen-associated proteins have been linked to heritable disorders, and changes in collagen levels have been associated with a wide range of diseases, including cancer. Yet despite extensive research, a full understanding of how cells assemble collagen fibrils remains elusive. Here, we review current models of collagen fibril self-assembly, and how cells might exert control over the self-assembly process to define the number, length and organisation of fibrils in tissues.
Original languageEnglish
Article number100079
JournalMatrix Biology Plus
Volume12
Early online date13 Jul 2021
DOIs
Publication statusPublished - 1 Dec 2021

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