Infected cell protein 0 functional domains and their coordination in herpes simplex virus replication

Table 1 Infected cell protein 0 functional domains

Domain	Location	Function in HSV-1 replication	Section	Ref.
ICP0 cis-elements
RING finger	aa 116-156	E3 ubiquitin ligase, degrading PML, Sp100, etc.	RING finger domain and E3 ubiquitin ligase activity	[63-65]
Proline-rich region	aa 241-553	Containing redundant ND10-fusion segments	Proline-rich region and ND10-fusion	[105]
NLS	aa 500-506	Nuclear localization	Nuclear localization domain and ICP0 nuclear/cytoplasmic translocation	[90]
Dimerization domain	aa 617-711	ICP0 self-dimerization, in vivo functions unclear	Dimerization	[115-117]
ND10-retention domain	aa 669-775	Retaining ICP0 at ND10	ND10-retention	[53]
SLSs			SUMO interaction motif and ICP0 substrate recognition	[113]
SLS-4	aa 361-367	Binding to SUMO-1/2/3, stimulating in vitro polyubiquitination
SLS-5, SLS-7	aa 651-655, 681-685	Binding to SUMO-1, cooperating with SLS-4
ICP0 binding partners
RNF8	T67	Degrading RNF8 to regulate DNA damage responses	RNF8	[42,43]
Cyclin D3	D199	Involved in nuclear-to-cytoplasmic translocation of ICP0	Cyclin D3	[46,133-135]
BMAL1	aa 20-241	Activating viral transcription via BMAL1/CLOCK	BMAL1	[48,140]
EF-1δ	aa 543-768	Inhibiting translation in vitro, in vivo functions unclear	EF-1δ interaction	[96]
USP7	K620/K624	USP7 degradation, Cell-dependent ICP0 stabilization,	USP7 interaction	[47,85,88,123]
CoREST	D671/E673	Dislodging HDAC from REST/CoREST/HDAC repressor	CoREST interaction	[49,124]
WDR11	N/A	Regulating virion assembly and egress	WD repeat protein 11	[143]

ICP0: Infected cell protein 0; HSV-1: Herpes simplex virus 1; RING: Really interesting new gene; ND10: Nuclear domains 10; PML: Promyelocytic leukemia; Sp100: Speckled 100 kDa; NLS: Nuclear localization signal; SLS: SIM-like sequence; BMAL1: Brain and muscle ARNT-like protein 1; EF-1δ: Elongation factor 1δ; USP7: Ubiquitin-specific protease 7; SUMO: Small ubiquitin-like modifier; CLOCK: Circadian locomotor output cycles kaput.