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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Bibliographic Details
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
Citations: Items that this one cites
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Summary: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.
ISSN:0973-7138
0250-5991
0973-7138
DOI:10.1007/s12038-024-00432-z