Hemicentin-mediated type IV collagen assembly strengthens juxtaposed basement membrane linkage.

Journal Article (Journal Article)

Basement membrane (BM) matrices surround and separate most tissues. However, through poorly understood mechanisms, BMs of adjacent tissue can also stably link to support organ structure and function. Using endogenous knock-in fluorescent proteins, conditional RNAi, optogenetics, and quantitative live imaging, we identified extracellular matrix proteins mediating a BM linkage (B-LINK) between the uterine utse and epidermal seam cell BMs in Caenorhabditis elegans that supports the uterus during egg-laying. We found that hemicentin is secreted by the utse and promotes fibulin-1 assembly to jointly initiate the B-LINK. During egg-laying, however, both proteins' levels decline and are not required for B-LINK maintenance. Instead, we discovered that hemicentin recruits ADAMTS9/20, which facilitates the assembly of high levels of type IV collagen that sustains the B-LINK during the mechanically active egg-laying period. This work reveals mechanisms underlying BM-BM linkage maturation and identifies a crucial function for hemicentin and fibulin-1 in initiating attachment and type IV collagen in strengthening this specialized form of tissue linkage.

Full Text

Duke Authors

Cited Authors

  • Gianakas, CA; Keeley, DP; Ramos-Lewis, W; Park, K; Jayadev, R; Kenny, IW; Chi, Q; Sherwood, DR

Published Date

  • January 2023

Published In

Volume / Issue

  • 222 / 1

Start / End Page

  • e202112096 -

PubMed ID

  • 36282214

Pubmed Central ID

  • PMC9597354

Electronic International Standard Serial Number (EISSN)

  • 1540-8140

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.202112096


  • eng