Multipronged regulation of autophagy and apoptosis: emerging role of TRIM proteins

Table 1 Structural features of TRIM proteins involved in autophagy and apoptosis

Autophagy	Apoptosis	Autophagy + Apoptosis	Classification	Domains [N–C]
	TRIM1		C-I-2	R-B1-B2-CC-COS-FN3-SPRY
TRIM63			C-II	R-B2-CC-COS-ACID
TRIM6, TRIM11, TRIM50	TRIM27	TRIM17, TRIM20, TRIM21, TRIM35, TRIM39, TRIM72	C-IV-1	R-B2-CC-PRY-SPRY
TRIM5	TRIM34	TRIM22	C-IV-2	R-B2-CC-SPRY
	TRIM69		C-IV-4	R-CC-PRY-SPRY
	TRIM14	TRIM16	C-IV-4?	B2-CC-PRY-SPRY
TRIM49	TRIM48		C-IV-5	R-B2-SPRY
	TRIM8, TRIM19		C-V-1	R-B1-B2-CC
TRIM31			C-V-2	R-B2-CC
		TRIM28	C-VI	R-B1-B2-CC-PHD-BROMO
		TRIM32	C-VII-3	R-B2-CC-NHL
		TRIM37	C-VIII	R-B2-CC-MATH
TRIM23			C-IX	R-B1-B2CC-ARF
TRIM59		TRIM13	C-XI	R-B2-CC-TM

Most TRIM proteins contain a RING-finger domain, one or two B-box (B1 or B2) domains, and a coiled-coil domain
TRIM proteins were classified as C-I to C-XI. TRIM proteins without a RING finger domain (no RING) were unclassified
R, RING-finger domain; B1, B-box domain 1; B2, B-box domain 2; CC, coiled-coil domain; COS, cos box; FN3, fibronectin type III repeat; PRY, PRY domain; SPRY, SPRY domain; ACID, acid-rich region; NHL, NHL domain; PHD, PHD domain; BROMO, bromodomain; MATH, Meprin and TRAF-homology domain; ARF, ADP-ribosylation factor family domain; TM, transmembrane domain. TRIM; Tripartite motif containing, RING, Really interesting new gene, C-I; Class I, N–C; N-terminal-C-terminal domain

ISSN: 1689-1392