Trans-endocytosis elicited by nectins transfers cytoplasmic cargo, including infectious material, between cells
Year: 2019
Type: article
Abstract: ABSTRACT Here, we show that cells expressing the adherens junction protein nectin-1 capture nectin-4-containing membranes from the surface of adjacent cells in a trans-endocytosis process. We find that internalized nectin-1–nectin-4 complexes follow the endocytic pathway. The nectin-1 cytoplasmic tail controls transfer: its deletion prevents trans-endocytosis, while its exchange with the nectin-4 tail reverses transfer direction. Nectin-1-expressing cells acquire dye-labeled cytoplasmic proteins synchronously with nectin-4, a process most active during cell adhesion. Some cytoplasmic cargo remains functional after transfer, as demonstrated with encapsidated genomes of measles virus (MeV). This virus uses nectin-4, but not nectin-1, as a receptor. Epithelial cells expressing nectin-4, but not those expressing another MeV receptor in its place, can transfer infection to nectin-1-expressing primary neurons. Thus, this newly discovered process can move cytoplasmic cargo, including infectious material, from epithelial cells to neurons. We name the process nectin-elicited cytoplasm transfer (NECT). NECT-related trans-endocytosis processes may be exploited by pathogens to extend tropism. This article has an associated First Person interview with the first author of the paper.
Source: Journal of Cell Science
DOI: 10.1242/jcs.235507
Authors: Alex R. Generous, Oliver J. Harrison, Regina B. Troyanovsky, Mathieu Mateo, Chanakha K. Navaratnarajah, Ryan C. Donohue, Christian K. Pfaller, Olga Alekhina, Alina P. Sergeeva, Indrajyoti Indra, Theresa Thornburg, Irina Kochetkova, Daniel D. Billadeau, Matthew P. Taylor, Sergey M. Troyanovsky, Barry Honig, Lawrence Shapiro, Roberto Cattaneo
Language: English
Subfield: Cell Biology
Domain: Life Sciences
Open Access status: green
Funders: National Science Foundation, Mayo Clinic, Merck, Life Sciences Research Foundation, National Institutes of Health, National Institute of General Medical Sciences, National Institute of Allergy and Infectious Diseases, National Institute of Arthritis and Musculoskeletal and Skin Diseases, Division of Molecular and Cellular Biosciences
Awards: G1047696237, Molecular basis of Cadherin Mediated Cell Adhesion, Inter-junctional signaling in epithelial junctional complex, G3555629282, G4784536417, G6462591831, Center for Zoonotic and Emerging Infectious Diseases, Measles virus C protein: polymerase interactions and innate immunity evasion, Inter-junctional signaling in epithelial junctional complex, Center for Zoonotic and Emerging Infectious Diseases, Measles virus airway epithelium entry, and rapid cell-to-cell spread, G9000047219, G9000143514, PhD Training Program in Virology and Gene Therapy, Cadherin Clusters and actin filaments
OpenAlex ID: W2963971270
