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
Language
- eng