title: B-LINK: a hemicentin, plakin, and integrin-dependent adhesion system that links tissues by connecting adjacent basement membranes.
abstract: Basement membrane (BM), a sheet-like form of extracellular matrix, surrounds most tissues. During organogenesis, specific adhesions between adjoining tissues frequently occur; however, their molecular basis is unclear. Using live-cell imaging and electron microscopy, we identify an adhesion system that connects the uterine and gonadal tissues through their juxtaposed BMs at the site of anchor cell (AC) invasion in C. elegans. We find that the extracellular matrix component hemicentin (HIM-4), found between BMs, forms punctate accumulations under the AC and controls BM linkage to promote rapid invasion. Through targeted screening, we identify the integrin-binding cytolinker plakin (VAB-10A) and integrin (INA-1/PAT-3) as key BM-BM linkage regulators: VAB-10A localizes to the AC-BM interface and tethers hemicentin to the AC while integrin promotes hemicentin punctae formation. Together, plakin, integrin, and hemicentin are founding components of a cell-directed adhesion system, which we name a BM-LINKage (B-LINK), that connects adjacent tissues through adjoining BMs.
authors.affiliation: Department of Biology, Duke University, Science Drive, Box 90388, Durham, NC 27708, USA.
authors.forename: Meghan A
authors.initials: MA
authors.lastname: Morrissey
authors.affiliation: Department of Biology, Duke University, Science Drive, Box 90388, Durham, NC 27708, USA.
authors.forename: Daniel P
authors.initials: DP
authors.lastname: Keeley
authors.affiliation: Department of Biology, Duke University, Science Drive, Box 90388, Durham, NC 27708, USA.
authors.forename: Elliott J
authors.initials: EJ
authors.lastname: Hagedorn
authors.affiliation: Department of Biology, Duke University, Science Drive, Box 90388, Durham, NC 27708, USA.
authors.forename: Shelly T H
authors.initials: STH
authors.lastname: McClatchey
authors.affiliation: Department of Biology, Duke University, Science Drive, Box 90388, Durham, NC 27708, USA.
authors.forename: Qiuyi
authors.initials: Q
authors.lastname: Chi
authors.affiliation: Center for C. elegans Anatomy, Albert Einstein College of Medicine, 1410 Pelham Parkway, Bronx, NY 10461, USA.
authors.forename: David H
authors.initials: DH
authors.lastname: Hall
authors.affiliation: Department of Biology, Duke University, Science Drive, Box 90388, Durham, NC 27708, USA. Electronic address: david.sherwood@duke.edu.
authors.forename: David R
authors.initials: DR
authors.lastname: Sherwood
mesh_terms: D000818:Animals; D001485:Basement Membrane / Q000378:metabolism*; D017173:Caenorhabditis elegans / Q000166:cytology / Q000378:metabolism*; D029742:Caenorhabditis elegans Proteins / Q000378:metabolism*; D002448:Cell Adhesion / Q000502:physiology; D002465:Cell Movement; D005109:Extracellular Matrix / Q000378:metabolism; D039641:Integrin beta Chains / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*
chemical_list: D029742:Caenorhabditis elegans Proteins; D039641:Integrin beta Chains; D008565:Membrane Proteins; C475260:VAB-10 protein, C elegans; C424064:him-4 protein, C elegans; C093515:pat-3 protein, C elegans