Tag: TRIM family

TRIM21

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TRIM21 is a unique intracellular antibody receptor and RING finger ubiquitin ligase that neutralises antibody‑coated viruses inside the cytosol. Through its PRY/SPRY domain and tripartite motif, TRIM21 triggers rapid ubiquitin‑mediated degradation and activates antiviral signalling pathways. Its roles in immunity, autoimmunity and biotechnology make TRIM21 a key regulator of intracellular defence.

TRIM25

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TRIM25 is a RING finger ubiquitin ligase that activates the antiviral sensor RIG‑I through K63‑linked ubiquitination. Its tripartite motif and PRY/SPRY domain enable precise regulation of innate immune signalling, interferon production and viral restriction. TRIM25 is targeted by multiple viruses, highlighting its importance as a frontline antiviral factor.

TRIM Family

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The TRIM family is a large group of single‑chain RING finger ubiquitin ligases that regulate innate immunity, antiviral defence, autophagy, transcription and protein quality control. Defined by their tripartite motif—RING, B‑box and coiled‑coil domains—TRIM proteins use diverse C‑terminal regions to achieve precise substrate specificity. Their roles in immunity, development and cancer make them key regulators of cellular homeostasis.

TRIM21

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TRIM21 is a unique intracellular antibody receptor and RING finger ubiquitin ligase that neutralises antibody‑coated viruses inside the cytosol. Through its PRY/SPRY domain and tripartite motif, TRIM21 triggers rapid ubiquitin‑mediated degradation and activates antiviral signalling pathways. Its roles in immunity, autoimmunity and biotechnology make TRIM21 a key regulator of intracellular defence.

TRIM25

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TRIM25 is a RING finger ubiquitin ligase that activates the antiviral sensor RIG‑I through K63‑linked ubiquitination. Its tripartite motif and PRY/SPRY domain enable precise regulation of innate immune signalling, interferon production and viral restriction. TRIM25 is targeted by multiple viruses, highlighting its importance as a frontline antiviral factor.

TRIM Family

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The TRIM family is a large group of single‑chain RING finger ubiquitin ligases that regulate innate immunity, antiviral defence, autophagy, transcription and protein quality control. Defined by their tripartite motif—RING, B‑box and coiled‑coil domains—TRIM proteins use diverse C‑terminal regions to achieve precise substrate specificity. Their roles in immunity, development and cancer make them key regulators of cellular homeostasis.