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Domain

Contains two homologous but distinct carbohydrate-binding domains.

Function

Beta-galactoside-binding lectin that acts as a sensor of membrane damage caused by infection and restricts the proliferation of infecting pathogens by targeting them for autophagy (PubMed:22246324, PubMed:28077878). Detects membrane rupture by binding beta-galactoside ligands located on the lumenal side of the endosome membrane; these ligands becoming exposed to the cytoplasm following rupture (PubMed:22246324, PubMed:28077878). Restricts infection by initiating autophagy via interaction with CALCOCO2/NDP52 (PubMed:22246324, PubMed:28077878). Required to restrict infection of bacterial invasion such as S.typhimurium (PubMed:22246324). Also required to restrict infection of Picornaviridae viruses (PubMed:28077878). Has a marked preference for 3'-O-sialylated and 3'-O-sulfated glycans (PubMed:21288902).

Tissue specificity

Ubiquitous. Selective expression by prostate carcinomas versus normal prostate and benign prostatic hypertrophy.

Cellular localization

  • Cytoplasmic vesicle
  • Cytoplasm
  • Cytosol

Alternative names

Galectin-8, Gal-8, Po66 carbohydrate-binding protein, Prostate carcinoma tumor antigen 1, Po66-CBP, PCTA-1, LGALS8

Target type

Proteins

Primary research area

Immunology & Infectious Disease

Molecular weight

35808Da

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