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Peer-reviewedCC BYEMBO Reports

TRIM62 facilitates influenza A virus entry by regulating WASH-dependent endosomal trafficking

  • Kajal Gupta1
  • Sampurna Pal1
  • Arpit Tyagi2
  • Roohani Bajaj1
  • Tejal Pathak1
  • Gaganpreet Kaur1
  • Deepak Sharma2
  • Indranil Banerjee1
  1. 1Department of Biological Sciences, Indian Institute of Science Education and Research (IISER) Mohali
  2. 2Protein Science and Engineering, Council of Scientific and Industrial Research-Institute of Microbial Technology
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Abstract

Endocytosis enables efficient cargo uptake while restricting uncontrolled cellular entry, yet how this balance is enforced during endocytic uptake remains poorly understood. Using influenza A virus (IAV) as a model cargo, we reveal a previously unrecognized role for the pentameric WASH complex (WASH) as a regulatory hub that integrates both permissive and inhibitory functions to control viral endocytosis. While the WASH subunits WASH1, CCDC53, SWIP, and Strumpellin collectively promote IAV entry, the FAM21 subunit acts antagonistically. Our data suggest that FAM21-mediated association of WASH with the retromer subunit VPS35 restrains the pro-endocytic activity of WASH, thereby limiting viral uptake. This inhibitory FAM21-VPS35 axis is counteracted by the E3 ubiquitin ligase TRIM62, which maintains WASH in a retromer-free, endocytically competent state that facilitates viral internalization. Beyond IAV, the WASH1 subunit and VPS35 also exhibit opposing roles during cholera toxin B uptake, suggesting a broader function in lipid raft-mediated endocytosis. Together, our findings establish WASH as a key determinant of IAV endocytosis, with TRIM62 modulating retromer-mediated restriction to facilitate productive viral entry.

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Cite

BibTeXRIS
BibTeX
@article{gupta2026trim62,
  title = {{TRIM62 facilitates influenza A virus entry by regulating WASH-dependent endosomal trafficking}},
  author = {Kajal Gupta and Sampurna Pal and Arpit Tyagi and Roohani Bajaj and Tejal Pathak and Gaganpreet Kaur and Deepak Sharma and Indranil Banerjee},
  journal = {EMBO Reports},
  year = {2026},
  month = sep,
  doi = {10.1038/s44319-026-00942-x},
  url = {https://doi.org/10.1038/s44319-026-00942-x},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - TRIM62 facilitates influenza A virus entry by regulating WASH-dependent endosomal trafficking
AU  - Kajal Gupta
AU  - Sampurna Pal
AU  - Arpit Tyagi
AU  - Roohani Bajaj
AU  - Tejal Pathak
AU  - Gaganpreet Kaur
AU  - Deepak Sharma
AU  - Indranil Banerjee
PY  - 2026
DA  - 2026/09/01
JO  - EMBO Reports
DO  - 10.1038/s44319-026-00942-x
UR  - https://doi.org/10.1038/s44319-026-00942-x
AB  - Endocytosis enables efficient cargo uptake while restricting uncontrolled cellular entry, yet how this balance is enforced during endocytic uptake remains poorly understood. Using influenza A virus (IAV) as a model cargo, we reveal a previously unrecognized role for the pentameric WASH complex (WASH) as a regulatory hub that integrates both permissive and inhibitory functions to control viral endocytosis. While the WASH subunits WASH1, CCDC53, SWIP, and Strumpellin collectively promote IAV entry, the FAM21 subunit acts antagonistically. Our data suggest that FAM21-mediated association of WASH with the retromer subunit VPS35 restrains the pro-endocytic activity of WASH, thereby limiting viral uptake. This inhibitory FAM21-VPS35 axis is counteracted by the E3 ubiquitin ligase TRIM62, which maintains WASH in a retromer-free, endocytically competent state that facilitates viral internalization. Beyond IAV, the WASH1 subunit and VPS35 also exhibit opposing roles during cholera toxin B uptake, suggesting a broader function in lipid raft-mediated endocytosis. Together, our findings establish WASH as a key determinant of IAV endocytosis, with TRIM62 modulating retromer-mediated restriction to facilitate productive viral entry.
SN  - 1469-3178
ER  -