Functional interactions between ubiquitin E2 enzymes and TRIM proteins

Luisa M. Napolitano, Ellis G. Jaffray, Ronald T. Hay, Germana Meroni

    Research output: Contribution to journalArticle

    57 Citations (Scopus)

    Abstract

    The TRIM (tripartite motif) family of proteins is characterized by the presence of the tripartite motif module, composed of a RING domain, one or two B-box domains and a coiled-coil region. TRIM proteins are involved in many cellular processes and represent the largest subfamily of RING-containing putative ubiquitin E3 ligases. Whereas their role as E3 ubiquitin ligases has been presumed, and in several cases established, little is known about their specific interactions with the ubiquitin-conjugating E2 enzymes or UBE2s. In the present paper, we report a thorough screening of interactions between the TRIM and UBE2 families. We found a general preference of the TRIM proteins for the D and E classes of UBE2 enzymes, but we also revealed very specific interactions between TRIM9 and UBE2G2, and TRIM32 and UBE2V1/2. Furthermore, we demonstrated that the TRIM E3 activity is only manifest with the UBE2 with which they interact. For most specific interactions, we could also observe subcellular co-localization of the TRIM involved and its cognate UBE2 enzyme, suggesting that the specific selection of TRIM-UBE2 pairs has physiological relevance. Our findings represent the basis for future studies on the specific reactions catalysed by the TRIM E3 ligases to determine the fate of their targets.

    Original languageEnglish
    Pages (from-to)309-319
    Number of pages11
    JournalBiochemical Journal
    Volume434
    DOIs
    Publication statusPublished - 1 Mar 2011

    Keywords

    • RING domain
    • tripartite motif protein (TRIM protein)
    • ubiquitin-conjugating E2 enzyme
    • ubiquitin E3 ligase
    • ubiquitylation
    • RING FINGER PROTEINS
    • DYSTROPHY TYPE 2H
    • CONJUGATING ENZYMES
    • LIGASE
    • E3
    • DEGRADATION
    • DOMAIN
    • MOTIF
    • SYSTEM
    • FAMILY

    Cite this

    Napolitano, Luisa M. ; Jaffray, Ellis G. ; Hay, Ronald T. ; Meroni, Germana. / Functional interactions between ubiquitin E2 enzymes and TRIM proteins. In: Biochemical Journal. 2011 ; Vol. 434. pp. 309-319.
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    Functional interactions between ubiquitin E2 enzymes and TRIM proteins. / Napolitano, Luisa M.; Jaffray, Ellis G.; Hay, Ronald T.; Meroni, Germana.

    In: Biochemical Journal, Vol. 434, 01.03.2011, p. 309-319.

    Research output: Contribution to journalArticle

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    T1 - Functional interactions between ubiquitin E2 enzymes and TRIM proteins

    AU - Napolitano, Luisa M.

    AU - Jaffray, Ellis G.

    AU - Hay, Ronald T.

    AU - Meroni, Germana

    PY - 2011/3/1

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    N2 - The TRIM (tripartite motif) family of proteins is characterized by the presence of the tripartite motif module, composed of a RING domain, one or two B-box domains and a coiled-coil region. TRIM proteins are involved in many cellular processes and represent the largest subfamily of RING-containing putative ubiquitin E3 ligases. Whereas their role as E3 ubiquitin ligases has been presumed, and in several cases established, little is known about their specific interactions with the ubiquitin-conjugating E2 enzymes or UBE2s. In the present paper, we report a thorough screening of interactions between the TRIM and UBE2 families. We found a general preference of the TRIM proteins for the D and E classes of UBE2 enzymes, but we also revealed very specific interactions between TRIM9 and UBE2G2, and TRIM32 and UBE2V1/2. Furthermore, we demonstrated that the TRIM E3 activity is only manifest with the UBE2 with which they interact. For most specific interactions, we could also observe subcellular co-localization of the TRIM involved and its cognate UBE2 enzyme, suggesting that the specific selection of TRIM-UBE2 pairs has physiological relevance. Our findings represent the basis for future studies on the specific reactions catalysed by the TRIM E3 ligases to determine the fate of their targets.

    AB - The TRIM (tripartite motif) family of proteins is characterized by the presence of the tripartite motif module, composed of a RING domain, one or two B-box domains and a coiled-coil region. TRIM proteins are involved in many cellular processes and represent the largest subfamily of RING-containing putative ubiquitin E3 ligases. Whereas their role as E3 ubiquitin ligases has been presumed, and in several cases established, little is known about their specific interactions with the ubiquitin-conjugating E2 enzymes or UBE2s. In the present paper, we report a thorough screening of interactions between the TRIM and UBE2 families. We found a general preference of the TRIM proteins for the D and E classes of UBE2 enzymes, but we also revealed very specific interactions between TRIM9 and UBE2G2, and TRIM32 and UBE2V1/2. Furthermore, we demonstrated that the TRIM E3 activity is only manifest with the UBE2 with which they interact. For most specific interactions, we could also observe subcellular co-localization of the TRIM involved and its cognate UBE2 enzyme, suggesting that the specific selection of TRIM-UBE2 pairs has physiological relevance. Our findings represent the basis for future studies on the specific reactions catalysed by the TRIM E3 ligases to determine the fate of their targets.

    KW - RING domain

    KW - tripartite motif protein (TRIM protein)

    KW - ubiquitin-conjugating E2 enzyme

    KW - ubiquitin E3 ligase

    KW - ubiquitylation

    KW - RING FINGER PROTEINS

    KW - DYSTROPHY TYPE 2H

    KW - CONJUGATING ENZYMES

    KW - LIGASE

    KW - E3

    KW - DEGRADATION

    KW - DOMAIN

    KW - MOTIF

    KW - SYSTEM

    KW - FAMILY

    U2 - 10.1042/BJ20101487

    DO - 10.1042/BJ20101487

    M3 - Article

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    SP - 309

    EP - 319

    JO - Biochemical Journal

    JF - Biochemical Journal

    SN - 0264-6021

    ER -