Dynein functions in galectin-3 mediated processes of clathrin-independent endocytosis

Multiple endocytic processes operate in cells in tandem to uptake multiple cargoes involved in diverse cellular functions, including cell adhesion and migration. The best-studied clathrin-mediated endocytosis (CME) involves the formation of a well-defined cytoplasmic clathrin coat to facilitate carg...

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Published in:Journal of biosciences 2024-02, Vol.49 (1), p.42, Article 42
Main Authors: Mayya, Chaithra, Hema Naveena, A, Sinha, Pankhuri, Bhatia, Dhiraj
Format: Article
Language:English
Subjects:
Antibodies
Biological Transport
Biomedical and Life Sciences
Biomedicine
Cargo
CD147 antigen
Cell adhesion
Cell Biology
Cell culture
Cell migration
Cell surface receptors
Clathrin
Cleavage
Cytoskeleton
Deformation
Dynein
Dyneins
Endocytosis
Endocytosis - genetics
Galectin 3 - genetics
Galectin-3
Glycolipids
Glycosphingolipids
Humidity
Invaginations
Kinases
Lectins
Life Sciences
Membranes
Microbiology
Penicillin
Plant Sciences
Plasma
Proteins
Roles
Transferrin
Zoology
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creator Mayya, Chaithra
Hema Naveena, A
Sinha, Pankhuri
Bhatia, Dhiraj
description Multiple endocytic processes operate in cells in tandem to uptake multiple cargoes involved in diverse cellular functions, including cell adhesion and migration. The best-studied clathrin-mediated endocytosis (CME) involves the formation of a well-defined cytoplasmic clathrin coat to facilitate cargo uptake. According to the glycolipid–lectin (GL–Lect) hypothesis, galectin-3 (Gal3) binds to glycosylated membrane receptors and glycosphingolipids (GSLs) to drive membrane bending and tubular membrane invaginations that undergo scission to form a morphologically distinct class of uptake structures, termed clathrin-independent carriers (CLICs). Which components from cytoskeletal machinery are involved in the scission of CLICs remains to be explored. In this study, we propose that dynein is recruited onto Gal3-induced tubular endocytic pits and provides the pulling force for friction-driven scission. The uptake of Gal3 and its cargoes (CD98/CD147) is significantly dependent on dynein activity, whereas only transferrin (CME marker) is slightly affected upon dynein inhibition. Our study reveals that Gal3 and Gal3-dependent (CD98 and CD147) clathrin-independent cargoes require dynein for the clathrin-independent endocytosis.
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subjects Antibodies
Biological Transport
Biomedical and Life Sciences
Biomedicine
Cargo
CD147 antigen
Cell adhesion
Cell Biology
Cell culture
Cell migration
Cell surface receptors
Clathrin
Cleavage
Cytoskeleton
Deformation
Dynein
Dyneins
Endocytosis
Endocytosis - genetics
Galectin 3 - genetics
Galectin-3
Glycolipids
Glycosphingolipids
Humidity
Invaginations
Kinases
Lectins
Life Sciences
Membranes
Microbiology
Penicillin
Plant Sciences
Plasma
Proteins
Roles
Transferrin
Zoology
title Dynein functions in galectin-3 mediated processes of clathrin-independent endocytosis
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