Functional interactions between ubiquitin E2 enzymes and TRIM proteins

TY - JOUR

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

Y1 - 2011/3/1

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

C2 - 21143188

SN - 0264-6021

VL - 434

SP - 309

EP - 319

JO - Biochemical Journal

JF - Biochemical Journal

ER -