Mitotic Prophase (Homo sapiens)

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3, 34, 38, 435, 37387, 118, 391, 21, 497, 1137, 5217, 22, 308, 482, 9, 25, 28, 29, 41...14, 18, 19, 23, 26...15, 533, 6, 13, 38, 43...15, 39, 537, 1110, 12, 16, 17, 22...cytosolp-T216,S274,S373-GORASP1p-S37-GOLGA2p-RAB1GTP p-T222,225-GORASP2BLZF1RAB2AGTP p-RAB1GTP GORASP1GOLGA2USO1RAB1GTP p-T333-NEK9 p-RAB1GTP Nup62 Complex p-3S,2T-NEK9 p-T216,S274,S373-GORASP1p-S37-GOLGA2p-RAB1GTPPLK1 Nuclear Pore Complex p-3S,2T-NEK9 p-S206-NEK6/ p-S195-NEK7 p-T161-CDK1CCNB1 p-RAB1GTP Golgi membraneEMD/TMPO/LEMD3/LEMD2Lamin dimers Nup62 Complex p-3S,T-NEK9 GORASP2BLZF1RAB2AGTP Cyclin B1phospho-Cdc2Cyclin B2phospho-Cdc2RAB2AGTP p-3S,2T-NEK9 EMD/TMPO/LEMD3/LEMD2Lamin dimersBANF1Chromatin p-S62-ARPP19/p-S67-ENSAPP2A-PPP2R2D Nuclear Pore Complex BANF1 p-S62-ARPP19/p-S67-ENSA Nup62 Complex p-3S,2T-NEK9 p-T216,S189,S274,S373-GORASP1p-S37-GOLGA2p-RAB1GTPPLK1 RAB1GTP ER to Golgi transport vesicle membraneRAB2AGTP USO1 homodimer Nup107 Complex PP2A-PPP2R2D USO1 homodimer p-T2,T3,S4-BANF1 PP2A-PPP2R2D CCNBp-T161-CDK1 p-T216,S274,S373-GORASP1p-S37-GOLGA2p-RAB1GTP Partially Disassembled NPC Nup107 Complex Chromatin p-3S,2T-NEK9NEK6/NEK7 nucleoplasmNup107 Complex AAAS BANF1 p-S37-GOLGA2 Mitotic G2-G2/M phasesNup45 p-S62-ARPP19/p-S67-ENSANup45 NUP85 Golgi cisternaeNUPL1-2 p-S62-ARPP19 GTP ADPNUP88 ENSAER to Golgi transport vesicle fused with cis-GolgiPOM121 RAE1 NUP62 TPR p-T216,S274,S373-GORASP1ADPNUP43 POM121 RANBP2 CCNB1 RAB2AStacked Golgi cisternaeCCNBp-T161-CDK1NUP37 Nuclear Pore Complex Nuclear Pore Complex p-Y204-MAPK3-3/p-T185,Y187-MAPK1 homodimerPPP2R2D BLZF1 CCNB2 ATPp-T161-CDK1CCNB1NUP35 NUPL2 NUP160 USO1 homodimerBLZF1 MASTLNUP210 GORASP2BLZF1RAB2AGTPNUP43 PLK1 NUP133 ADPp-S37-GOLGA2 NUP205p-T194,T207,T741-MASTLGORASP2NUP88 NUPL1-2 NUPL2 p-S29,T210,T333,S750,S869-NEK9ATPARPP19p-S189,T216,S274,S373-GORASP1NUP153 NUP98-5 ATPAAAS SEH1L-2 POM121 ER to Golgi transport vesiclep-T216,S274,S373-GORASP1p-S37-GOLGA2p-RAB1GTPPLK1SEH1L-2 p-4S,3T-NUP98GTP ADPp-S67-ENSANUP43 TPR ADPChromatinNUP50 PP2A-PPP2R2DADPNUP54 ATPp-S29,T210,T333,S750,S869-NEK9p-T2,T3,S4-BANF1 NUP155 p-S62-ARPP19NEK6/NEK7p-T2,T3,S4-BANF1NUP107 VRK1/VRK2ATPPLK1 ATPp-T333-NEK9NUP153 Partially Disassembled NPCNUP210 NUP93 ATPNUP98-5 Nup45 NUP188NUP133 CCNB1 NUP37 RAE1 NUP98-5 ADPNUP214 GTP ATPp-T222,225-GORASP2BLZF1RAB2AGTPp-T216,S274,S373-GORASP1NUP155 SEH1L-2 NUP155 p-T161-CDK1 NUP133 NUP210 ATPGTP p-3S,2T-NEK9NEK6/NEK7ATPRAE1 NUP153 NUP205RANBP2 NUP62 NUP160 NUPL2 EMD/TMPO/LEMD3/LEMD2Lamin dimersp-T161-CDK1 NUP93 ADPEMD/TMPO/LEMD3/LEMD2Lamin dimersBANF1Chromatinp-3S,2T-NEK9 p-S206-NEK6/ p-S195-NEK7RANBP2 ATPNUP50 NUP107 ADPPPP2R2D GTP NUP62 NUP35 p-S29,T333,S750,S869-NEK9NUPL1-2 NUP205USO1 GOLGA2 GORASP1p-S29,T210,T333,S750,S869-NEK9p-3S,T-NEK9GTP NUP214 p-4S,3T-NUP98p-T216,S274,S373-GORASP1p-S37-GOLGA2p-RAB1GTPNUP188p-T222,T225-GORASP2p-T333-NEK9GORASP1GOLGA2USO1RAB1GTPADPp-S37-GOLGA2 ADPATPp-S67-ENSATPR NUP107 NUP93 USO1 NUP37 AAAS p-3S,2T-NEK9NUP188NUP50 NUP85 NUP160 NUP54 NUP35 NUP214 RAB2Ap-S62-ARPP19/p-S67-ENSAPP2A-PPP2R2DNUP85 p-T216,S189,S274,S373-GORASP1p-S37-GOLGA2p-RAB1GTPPLK1NUP88 PLK1NUP54 ADP15, 39, 534, 20, 5439, 534, 20, 544, 20, 54538, 398, 39


Description

During prophase, the chromatin in the nucleus condenses, and the nucleolus disappears. Centrioles begin moving to the opposite poles or sides of the cell. Some of the fibers that extend from the centromeres cross the cell to form the mitotic spindle. Original Pathway at Reactome: http://www.reactome.org/PathwayBrowser/#DB=gk_current&FOCUS_SPECIES_ID=48887&FOCUS_PATHWAY_ID=68875

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Bibliography

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History

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CompareRevisionActionTimeUserComment
114619view16:07, 25 January 2021ReactomeTeamReactome version 75
113067view11:12, 2 November 2020ReactomeTeamReactome version 74
112302view15:22, 9 October 2020ReactomeTeamReactome version 73
101200view11:10, 1 November 2018ReactomeTeamreactome version 66
100738view20:34, 31 October 2018ReactomeTeamreactome version 65
100282view19:11, 31 October 2018ReactomeTeamreactome version 64
99828view15:55, 31 October 2018ReactomeTeamreactome version 63
99385view14:33, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
93896view13:43, 16 August 2017ReactomeTeamreactome version 61
93469view11:24, 9 August 2017ReactomeTeamreactome version 61
87979view13:19, 25 July 2016RyanmillerOntology Term : 'cell cycle pathway, mitotic' added !
87974view13:17, 25 July 2016RyanmillerOntology Term : 'regulatory pathway' added !
86563view09:21, 11 July 2016ReactomeTeamreactome version 56
83248view10:30, 18 November 2015ReactomeTeamVersion54
81354view12:52, 21 August 2015ReactomeTeamVersion53
76823view08:04, 17 July 2014ReactomeTeamFixed remaining interactions
76527view11:50, 16 July 2014ReactomeTeamFixed remaining interactions
75860view09:51, 11 June 2014ReactomeTeamRe-fixing comment source
75560view10:35, 10 June 2014ReactomeTeamReactome 48 Update
74915view13:44, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74559view08:36, 30 April 2014ReactomeTeamNew pathway

External references

DataNodes

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NameTypeDatabase referenceComment
AAAS ProteinQ9NRG9 (Uniprot-TrEMBL)
ADPMetaboliteCHEBI:16761 (ChEBI)
ARPP19ProteinP56211 (Uniprot-TrEMBL)
ATPMetaboliteCHEBI:15422 (ChEBI)
BANF1 ProteinO75531 (Uniprot-TrEMBL)
BLZF1 ProteinQ9H2G9 (Uniprot-TrEMBL)
CCNB p-T161-CDK1ComplexREACT_148199 (Reactome)
CCNB1 ProteinP14635 (Uniprot-TrEMBL)
CCNB2 ProteinO95067 (Uniprot-TrEMBL)
ChromatinREACT_152305 (Reactome)
EMD/TMPO/LEMD3/LEMD2

Lamin dimers BANF1

Chromatin		ComplexREACT_161104 (Reactome)
EMD/TMPO/LEMD3/LEMD2 Lamin dimersComplexREACT_161442 (Reactome)
ENSAProteinO43768 (Uniprot-TrEMBL)
ER to Golgi transport vesicle fused with cis-GolgiREACT_148231 (Reactome)
ER to Golgi transport vesicleREACT_148289 (Reactome)
GOLGA2 ProteinQ08379 (Uniprot-TrEMBL)
GORASP1

GOLGA2 USO1 RAB1

GTP		ComplexREACT_148011 (Reactome)
GORASP1ProteinQ9BQQ3 (Uniprot-TrEMBL)
GORASP2

BLZF1 RAB2A

GTP		ComplexREACT_148276 (Reactome)
GORASP2ProteinQ9H8Y8 (Uniprot-TrEMBL)
GTP MetaboliteCHEBI:15996 (ChEBI)
Golgi cisternaeREACT_148019 (Reactome)
MASTLProteinQ96GX5 (Uniprot-TrEMBL)
Mitotic G2-G2/M phasesPathwayWP1859 (WikiPathways)
NEK6/NEK7ProteinREACT_161237 (Reactome)
NUP107 ProteinP57740 (Uniprot-TrEMBL)
NUP133 ProteinQ8WUM0 (Uniprot-TrEMBL)
NUP153 ProteinP49790 (Uniprot-TrEMBL)
NUP155 ProteinO75694 (Uniprot-TrEMBL)
NUP160 ProteinQ12769 (Uniprot-TrEMBL)
NUP188ProteinQ5SRE5 (Uniprot-TrEMBL)
NUP205ProteinQ92621 (Uniprot-TrEMBL)
NUP210 ProteinQ8TEM1 (Uniprot-TrEMBL)
NUP214 ProteinP35658 (Uniprot-TrEMBL)
NUP35 ProteinQ8NFH5 (Uniprot-TrEMBL)
NUP37 ProteinQ8NFH4 (Uniprot-TrEMBL)
NUP43 ProteinQ8NFH3 (Uniprot-TrEMBL)
NUP50 ProteinQ9UKX7 (Uniprot-TrEMBL)
NUP54 ProteinQ7Z3B4 (Uniprot-TrEMBL)
NUP62 ProteinP37198 (Uniprot-TrEMBL)
NUP85 ProteinQ9BW27 (Uniprot-TrEMBL)
NUP88 ProteinQ99567 (Uniprot-TrEMBL)
NUP93 ProteinQ8N1F7 (Uniprot-TrEMBL)
NUP98-5 ProteinP52948-5 (Uniprot-TrEMBL)
NUPL1-2 ProteinQ9BVL2-1 (Uniprot-TrEMBL)
NUPL2 ProteinO15504 (Uniprot-TrEMBL)
Nuclear Pore Complex ComplexREACT_164645 (Reactome)
Nuclear Pore Complex ComplexREACT_5542 (Reactome)
Nup45 ProteinQ9BVL2-2 (Uniprot-TrEMBL)
PLK1 ProteinP53350 (Uniprot-TrEMBL)
PLK1ProteinP53350 (Uniprot-TrEMBL)
POM121 ProteinQ96HA1 (Uniprot-TrEMBL)
PP2A-PPP2R2DComplexREACT_150946 (Reactome)
PPP2R2D ProteinQ66LE6 (Uniprot-TrEMBL)
Partially Disassembled NPCComplexREACT_165314 (Reactome)
RAB2AProteinP61019 (Uniprot-TrEMBL)
RAE1 ProteinP78406 (Uniprot-TrEMBL)
RANBP2 ProteinP49792 (Uniprot-TrEMBL)
SEH1L-2 ProteinQ96EE3-2 (Uniprot-TrEMBL)
Stacked Golgi cisternaeREACT_148001 (Reactome)
TPR ProteinP12270 (Uniprot-TrEMBL)
USO1 ProteinO60763 (Uniprot-TrEMBL)
USO1 homodimerComplexREACT_148109 (Reactome)
VRK1/VRK2ProteinREACT_161012 (Reactome)
p-3S,2T-NEK9 p-S206-NEK6/ p-S195-NEK7ComplexREACT_161203 (Reactome)
p-3S,2T-NEK9 NEK6/NEK7ComplexREACT_161431 (Reactome)
p-3S,2T-NEK9ComplexREACT_160680 (Reactome)
p-3S,T-NEK9ComplexREACT_160970 (Reactome)
p-4S,3T-NUP98ProteinREACT_164794 (Reactome)
p-4S,3T-NUP98ProteinREACT_164946 (Reactome)
p-S189,T216,S274,S373-GORASP1ProteinQ9BQQ3 (Uniprot-TrEMBL)
p-S29,T210,T333,S750,S869-NEK9ProteinQ8TD19 (Uniprot-TrEMBL)
p-S29,T333,S750,S869-NEK9ProteinQ8TD19 (Uniprot-TrEMBL)
p-S37-GOLGA2 ProteinQ08379 (Uniprot-TrEMBL)
p-S62-ARPP19 ProteinP56211 (Uniprot-TrEMBL)
p-S62-ARPP19/p-S67-ENSA PP2A-PPP2R2DComplexREACT_150546 (Reactome)
p-S62-ARPP19/p-S67-ENSAProteinREACT_150512 (Reactome)
p-S62-ARPP19ProteinP56211 (Uniprot-TrEMBL)
p-S67-ENSAProteinO43768 (Uniprot-TrEMBL)
p-T161-CDK1 CCNB1ComplexREACT_6540 (Reactome)
p-T161-CDK1 ProteinP06493 (Uniprot-TrEMBL)
p-T194,T207,T741-MASTLProteinQ96GX5 (Uniprot-TrEMBL)
p-T2,T3,S4-BANF1 ProteinO75531 (Uniprot-TrEMBL)
p-T2,T3,S4-BANF1ComplexREACT_160332 (Reactome)
p-T216,S189,S274,S373-GORASP1

p-S37-GOLGA2 p-RAB1 GTP

PLK1		ComplexREACT_148029 (Reactome)
p-T216,S274,S373-GORASP1

p-S37-GOLGA2 p-RAB1 GTP

PLK1		ComplexREACT_148515 (Reactome)
p-T216,S274,S373-GORASP1

p-S37-GOLGA2 p-RAB1

GTP		ComplexREACT_148500 (Reactome)
p-T216,S274,S373-GORASP1ProteinQ9BQQ3 (Uniprot-TrEMBL)
p-T222,225-GORASP2

BLZF1 RAB2A

GTP		ComplexREACT_148269 (Reactome)
p-T222,T225-GORASP2ProteinQ9H8Y8 (Uniprot-TrEMBL)
p-T333-NEK9ProteinQ8TD19 (Uniprot-TrEMBL)
p-T333-NEK9ComplexREACT_161099 (Reactome)
p-Y204-MAPK3-3/p-T185,Y187-MAPK1 homodimerComplexREACT_148329 (Reactome)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
ADPArrowREACT_147845 (Reactome)
ADPArrowREACT_147850 (Reactome)
ADPArrowREACT_147881 (Reactome)
ADPArrowREACT_150207 (Reactome)
ADPArrowREACT_150326 (Reactome)
ADPArrowREACT_150461 (Reactome)
ADPArrowREACT_160129 (Reactome)
ADPArrowREACT_160217 (Reactome)
ADPArrowREACT_160221 (Reactome)
ADPArrowREACT_160237 (Reactome)
ADPArrowREACT_163651 (Reactome)
ADPArrowREACT_163999 (Reactome)
ARPP19REACT_150326 (Reactome)
ATPREACT_147845 (Reactome)
ATPREACT_147850 (Reactome)
ATPREACT_147881 (Reactome)
ATPREACT_150207 (Reactome)
ATPREACT_150326 (Reactome)
ATPREACT_150461 (Reactome)
ATPREACT_160129 (Reactome)
ATPREACT_160217 (Reactome)
ATPREACT_160221 (Reactome)
ATPREACT_160237 (Reactome)
ATPREACT_163651 (Reactome)
ATPREACT_163999 (Reactome)
CCNB p-T161-CDK1REACT_147845 (Reactome)
CCNB p-T161-CDK1REACT_160217 (Reactome)
CCNB p-T161-CDK1REACT_163651 (Reactome)
ChromatinArrowREACT_160221 (Reactome)
EMD/TMPO/LEMD3/LEMD2

Lamin dimers BANF1

Chromatin		REACT_160221 (Reactome)
EMD/TMPO/LEMD3/LEMD2 Lamin dimersArrowREACT_160221 (Reactome)
ENSAREACT_150207 (Reactome)
GORASP1

GOLGA2 USO1 RAB1

GTP		REACT_147845 (Reactome)
GORASP2

BLZF1 RAB2A

GTP		REACT_147850 (Reactome)
MASTLREACT_150461 (Reactome)
NEK6/NEK7REACT_160202 (Reactome)
Nuclear Pore Complex ArrowREACT_163651 (Reactome)
Nuclear Pore Complex REACT_163651 (Reactome)
Nuclear Pore Complex REACT_163999 (Reactome)
PLK1REACT_147849 (Reactome)
PLK1REACT_160237 (Reactome)
PP2A-PPP2R2DREACT_150301 (Reactome)
Partially Disassembled NPCArrowREACT_163999 (Reactome)
REACT_147730 (Reactome) USO1 (p115) protein, localizing to membranes of ER to Golgi transport vesicles, binds GOLGA2 (GM130), localizing to membranes of cis-Golgi cisternae. Binding of USO1 to GOLGA2 enables tethering of ER to Golgi transport vesicles to cis-Golgi cisternae, and is facilitated by a Ras-related GTPase RAB1. Fusion of ER to Golgi transport vesicles with cis-Golgi succeeds tethering and depends on STX5 (syntaxin-5). In mitosis, phosphorylation of GOLGA2 by cyclin B-activated CDK1 prevents USO1 docking. This results in cessation of ER to Golgi transport. Halting ER to Golgi transport increases the number of transport vesicles at the expense of Golgi cisternae, since transport vesicles keep budding from the ER but are unable to fuse with Golgi cisternae and deliver their content (Lowe et al. 1998, Seeman et al. 2000, Diao et al. 2008).
REACT_147809 (Reactome) Adjacent cisternae of the Golgi apparatus are stacked and linked by tubules to from a Golgi ribbon (Nakamura et al. 2012). GORASP1 (GRASP65), a protein localizing to membranes of cis-Golgi cisternae, enables stacking by in trans dimerization/oligomerization through its PDZ domains (Tang et al. 2010). In mitosis, GORASP1 is phosphorylated by CDK1 and PLK1 (Preisinger et al. 2005). PLK1-mediated phosphorylation of GORASP1 prevents stacking of Golgi cisternae and contributes to unlinking and fragmentation of the Golgi apparatus, probably by interfering with GORASP1 oligomerization (Wang et al. 2003, Sengupta and Linstedt 2010). Similarly, GORASP2 (GRASP55), localized to median Golgi cisternae, promotes stacking by trans-oligomerization. Trans-oligomerization of GORASP2 is prevented by mitotic phosphorylation of GORASP2 downstream of MEK/ERK cascade, and contributes to the Golgi fragmentation in prophase (Xiang and Wang 2010).
REACT_147845 (Reactome) GORASP1 (GRASP65) and GOLGA2 (GM130) form a complex on cis-Golgi membranes. RAB1A or RAB1B, small RAS GTP-ases, can also associate with this complex through interaction with GOLGA2 (Moyer et al. 2001, Weide et al. 2001). GOLGA2 provides a docking site for the USO1 (p115) homodimer (Nakamura et al. 1995, Seeman et al. 2000). RAB1 also participates in this interaction and facilitates it when in the GTP-bound state (Moyer et al. 2001). Binding of USO1 to GORASP1:GOLGA2:RAB1:GTP complex enables fusion of vesicles originating in the endoplasmic reticulum (ER) with cisternae of cis-Golgi.
In mitotic prophase, CDK1 (CDC2) in complex with either CCNB1 (cyclin B1) or CCNB2 (cyclin B2), as both CCNB1 and CCNB2 can localize to Golgi (Jackman et al. 1995, Draviam et al. 2001), phosphorylates GORASP1, GOLGA2 and RAB1 (Bailly et al. 1991, Lowe et al. 1998, Preisinger et al. 2005). Phosphorylation of GOLGA2 and RAB1 impairs their association with USO1, which inhibits thethering and subsequent fusion of ER-originating vesicles with cis-Golgi cisternae, resulting in cessation of ER to Golgi protein trafficking at the start of mitosis and increase in the number of Golgi trafficking vesicles at the expense of Golgi cisternae (Lowe et al. 1998, Seeman et al. 2000, Moyer et al. 2001, Diao et al. 2008).
REACT_147849 (Reactome) Phosphorylation of GORASP1 (GRASP65) by cyclin B-associated CDK1 creates a docking site for PLK1. PLK1 is also able to bind to CDK1-phosphorylated RAB1, but not to CDK1-phosphorylated GOLGA2 (Preisinger et al. 2005).
REACT_147850 (Reactome) GORASP2 (GRASP55) localizes to the median region of Golgi, where it forms a complex with BLZF1 (Golgin 45) and RAB2A GTPase (Short et al. 2001). Similar to GORASP1, GORASP2 is involved in the maintenance of Golgi structure and positively regulates stacking of Golgi cisternae (Xiang and Wang 2010). In addition, GORASP2, probably through its association with RAB2A GTPase, regulates trafficking through the Golgi (Short et al. 2001). In G2 and mitotic prophase, GORASP2 is phosphorylated by MEK1/2 activated MAP kinases. Monophosphorylated MAPK3 (ERK1) isoform, MAPK3 3 i.e. ERK1b (known as ERK1c in rat), likely activated by a MEK1 isoform MEK1b (Shaul et al. 2009), as well as MAPK1 (ERK2) are implicated in GORASP2 phosphorylation during mitosis (Jesch et al. 2001, Colanzi et al. 2003, Shaul and Seger 2006, Feinstein and Linstedt 2007, Duran et al. 2008, Feinstein and Linstedt 2008). Threonine residues T222 and T225 were implicated as targets of MAPK mediated GORASP2 phosphorylation in studies that used directional mutagenesis (Jesch et al. 2001, Feinstein and Linstedt 2008). However both T222 and T225 were simultaneously mutated in these studies and their roles have not been individually investigated. Using mass spectroscopy, T225 but not T222 was identified as a GORASP2 residue phosphorylated by mitotic cytosol (Duran et al. 2008). T249 residue of GORASP2 was also phosphorylated by mitotic cytosol, but the involvement of ERKs in T249 phosphorylation has not been examined (Duran et al. 2008).
REACT_147881 (Reactome) CDK1-mediated phosphorylation of GORASP1 (GRASP65) enables GORASP1 to recruit PLK1 (Preisinger et al. 2005). PLK1 phosphorylates GORASP1 on serine residue S189 (Sengupta and Linstedt 2010). This serine residue is near the GORASP1 region involved in GORASP1 dimerization and oligomerization, a process underlying the stacking of cis-Golgi cisternae (Wang et al. 2003). The phosphorylation of S189 by PLK1 impairs Golgi cisternae stacking (tethering), contributing to Golgi unlinking and fragmentation in mitosis, probably by preventing formation of GORASP1 dimers and oligomers (Sutterlin et al. 2001, Sengupta and Linstedt, 2010). Two other potential phosphorylation sites that match PLK1 substrate consensus sequence exist in GORASP1, but their functional significance has not yet been examined (Sengupta and Linstedt, 2010).
REACT_150207 (Reactome) MASTL (GWL) activates ENSA by phosphorylating it on serine residue S67 (Mochida et al. 2010, Gharbi-Ayachi et al. 2010).
REACT_150301 (Reactome) ARPP19 and ENSA, activated by MASTL (GWL) mediated phosphorylation, bind and inhibit PP2A complexed with the regulatory subunit PPP2R2D (B55-delta). Inhibition of PP2A-PPP2R2D phosphatase activity allows mitotis entry and mainetance by preventing dephosphorylation of CDK1 mitotic targets (Mochida et al. 2010, Gharbi-Ayachi et al. 2010).
REACT_150326 (Reactome) MASTL (GWL i.e. Greatwall kinase) phosphorylates ARPP19 on serine residue S62 (Gharbi-Ayachi et al. 2010). S62 of human ARPP19 corresponds to serine residue S67 of Xenopus Arpp19, which is phosphorylated by Xenopus Mastl (Mochida et al. 2010).
REACT_150461 (Reactome) At the beginning of mitosis, MASTL (GWL, Greatwall kinase) is activated by phosphorylation at several key sites. Many of these sites, including functionally important threonine residues T194, T207 and T741 (corresponding to Xenopus residues T193, T206 and T748), are proline directed, matching CDK1 consensus sequence, and thus probably phosphorylated by CDK1, as shown by in vitro studies (Yu et al. 2006. Blake-Hodek et al. 2012). Phosphorylation of the serine residue S875 (S883 in Xenopus) is implicated as critical for the mitotic function of MASTL (Vigneron et al. 2011) and likely occurs through autophosphorylation (Blake-Hodek et al. 2012). Other kinases, such as PLK1 (Vigneron et al. 2011) and other MASTL phosphorylation sites may also be involved in mitotic activation of MASTL (Yu et al. 2006, Vigneron et al. 2011, Blake-Hodek et al. 2012). Phosphorylation of the serine residue S102 (S101 in Xenopus) is functionally important but the responsible kinase has not been identified (Blake-Hodek et al. 2012).
REACT_160129 (Reactome) NEK9, activated by CDK1- and PLK1-mediated phosphorylation, phosphorylates NEK6 on serine residue S206, and NEK7 on serine residue S195. S206 and S195 are located in the activation loop of NEK6 and NEK7, respectively. NEK6 activation is dependent on S206 phosphorylation, although phosphorylation at threonine T202 may augment NEK6 kinase activity. NEK7 activity also depends on phosphorylation of S195. NEK9 remains tightly associated with NEK6 (as well as NEK7) after phosphorylation, and may direct NEK6/NEK7 to specific target (Belham et al. 2003). In addition, irrespective of phosphorylation, binding of the non-catalytic C-terminus of NEK9 to NEK7 (as well as NEK6), relieves autoinhibitory conformation of NEK7/NEK6. The autoinhibitory conformation of NEK7 depends on the formation of a hydrogen bond between tyrosine Y97 (tyrosine Y108 in NEK6) and leucine L180. This Y97-involving hydrogen bond prevents the formation of a salt bridge between lysine K63 and glutamate E82 of NEK7, which is essential for catalysis. Binding of NEK9 is thought to disrupt the hydrogen bond between Y97 and L180 of NEK7 (Y108 and L191 of NEK6) and allow NEK7/NEK6 to achieve active conformation (Richards et al. 2009).
REACT_160202 (Reactome) NEK9 forms a tight complex with NEK6 or NEK7 (Roig et al. 2002, Belham et al. 2003) in the cytosol.
REACT_160217 (Reactome) NEK9 functions as a homodimer and becomes catalytically active in mitosis through phosphorylation (Roig et al. 2002). While threonine T333 of NEK9 is phosphorylated in both interphase and mitotic cells (Roig et al. 2005, Bertran et al. 2011), serine residues S29, S750 and S869 of NEK9 are phosphorylated only in mitotic cells. S29, S750 and S869 sites are proline directed and match the CDK1 consensus sequence (Bertran et al. 2011). CDK1:CCNB complex was shown to phosphorylate NEK9 in vitro (Roig et al. 2002).
REACT_160221 (Reactome) BANF1 (BAF i.e. barrier-to-autointegration factor) is a DNA-binding protein that was initially discovered as a regulator of retroviral integration (Lee and Craigie 1994, Lee and Craigie 1998). BANF1 (BAF) binds DNA non-specifically as a homodimer (Zheng et al. 2000). Proteins of the inner nuclear membrane that possess a LEM domain, TMPO (LAP2beta), EMD (emerin), LEMD3 (MAN1) and LEMD2 (LEM2), form three-way complexes with BANF1 and lamins - intermediary filaments of the nucleoplasm (Shumaker et al. 2001, Holaska et al. 2003, Mansharamani and Wilson 2005, Brachner et al. 2005). These complexes are thought to be important for the structure of the nuclear lamina and also enable attachment of chromatin to the nuclear envelope (Haraguchi et al. 2001, Dechat et al. 2004).

In mitosis, VRK1 (and to a lesser extent VRK2) serine/threonine kinase phosphorylates BANF1 (BAF) on serine residue S4 and threonine residues T2 and T3 (Nichols et al. 2006, Gorjanacz et al. 2007, Asencio et al. 2012). Only VRK2 isoform VRK2-2 which can localize to the nucleus (Blanco et al. 2006) is annotated as BANF1 kinase. Phosphorylated BANF1 (BAF) dissociates from chromatin and the inner nuclear membrane proteins (Bengtsson and Wilson 2006), allowing chromatin to detach from the nuclear envelope.

VRK1 and VRK2 are autophoshorylated but not all autophosphorylation sites have been mapped and the impact of autohosphorylation on catalytic activity has not been determined.
REACT_160237 (Reactome) NEK9 serine residues S29, S750 and S869, which are likely targets of CDK1:CCNB-mediated phosphorylation in mitosis, can be recognized by the polo-box domain (PBD) of PLK1 when phosphorylated. Phosphorylation of S869 appears to be crucial for the interaction of NEK9 and PLK1 (Bertran et al. 2011). PLK1 phosphorylates threonine T210 of NEK9 in vitro. T210 is located in the kinase activation loop of NEK9 and T210 phosphorylation is necessary for NEK9 kinase activity. While T210 can be autophosphorylated in vitro, when NEK9 is incubated in the presence of excess ATP and Mg2+ (Roig et al. 2005), mitotic phosphorylation of T210 requires both CDK1 and PLK1 activity (Bertran et al. 2011).
REACT_163651 (Reactome) CDK1 activity promotes the nuclear pore complex (NPC) disassembly in mitosis (Muhlhausser and Kutay 2007). While NUP98 is probably not the only nucleoporin phosphorylated by CDK1 at mitotic entry, NUP98 is the best characterized CDK1 target among nuclear pore complex components. NUP98 threonine residues T529, T536, and T653, as well as serine residues S595 and S606 were found to be phosphorylated when NUP98 was isolated from mitotic HeLa cells (human cervical carcinoma cell line); these five sites match the CDK1 target site consensus and are phosphorylated by CDK1:CCNB in vitro (Laurell et al. 2011). The NUP98 splicing isoform NUP98-4 was used in the study by Laurell et al. 2011 and the indicated positions of phosphorylated amino acid residues refer to this isoform. An additional splicing isoform NUP98-3, the product of an alternative splicing site in exon10 of the NUP98 gene, which is 17 amino acids longer than NUP98-4, could also be a part of the NPC. CDK1-phosphorylated residues in NUP98-3 would be threonines T546, T553 and T670, and serines S612 and S623.
REACT_163999 (Reactome) Phosphorylation of NUP98 by NEK6 (and/or NEK7) promotes nuclear envelope permeabilization by initiating nuclear pore complex (NPC) disassembly. Two NUP98 serine residues, S591 and S822 (referring to NUP98 splice variant NUP98-4; these residues correspond to S608 and S839 of NUP98 splice variant NUP98-3), are phosphorylated on NUP98 isolated from mitotic HeLa cells (human cervical cancer cell line). These serine residues match the NEK6 target site consensus and are phosphorylated by NEK6 in vitro. Both sites can also be phosphorylated in vitro by NEK7 and weakly by NEK2. As NEK7 but not NEK2 was shown to be involved, with NEK6, in nuclear envelope permeabilization, NEK2 is not shown as the NUP98 kinase. Phosphorylated NUP98 dissociates from the NPC (Laurell et al. 2011). As NUP98 localizes to both sides of the NPC, cytosolic and nucleoplasmic (Griffis et al. 2003), the reaction shows a portion of NUP98 being released to the cytosol, and a portion of NUP98 dissociating into the nucleus, similar to what is observed by immunocytochemistry (Laurell et al. 2011).
USO1 homodimerArrowREACT_147845 (Reactome)
VRK1/VRK2REACT_160221 (Reactome)
p-3S,2T-NEK9 p-S206-NEK6/ p-S195-NEK7ArrowREACT_160129 (Reactome)
p-3S,2T-NEK9 p-S206-NEK6/ p-S195-NEK7REACT_163999 (Reactome)
p-3S,2T-NEK9 NEK6/NEK7REACT_160129 (Reactome)
p-3S,2T-NEK9ArrowREACT_160237 (Reactome)
p-3S,2T-NEK9REACT_160202 (Reactome)
p-3S,T-NEK9ArrowREACT_160217 (Reactome)
p-3S,T-NEK9REACT_160237 (Reactome)
p-4S,3T-NUP98ArrowREACT_163999 (Reactome)
p-S62-ARPP19/p-S67-ENSAREACT_150301 (Reactome)
p-S62-ARPP19ArrowREACT_150326 (Reactome)
p-S67-ENSAArrowREACT_150207 (Reactome)
p-T161-CDK1 CCNB1REACT_150461 (Reactome)
p-T194,T207,T741-MASTLArrowREACT_150461 (Reactome)
p-T194,T207,T741-MASTLREACT_150207 (Reactome)
p-T194,T207,T741-MASTLREACT_150326 (Reactome)
p-T2,T3,S4-BANF1ArrowREACT_160221 (Reactome)
p-T216,S189,S274,S373-GORASP1

p-S37-GOLGA2 p-RAB1 GTP

PLK1		ArrowREACT_147881 (Reactome)
p-T216,S189,S274,S373-GORASP1

p-S37-GOLGA2 p-RAB1 GTP

PLK1		TBarREACT_147809 (Reactome)
p-T216,S274,S373-GORASP1

p-S37-GOLGA2 p-RAB1 GTP

PLK1		REACT_147881 (Reactome)
p-T216,S274,S373-GORASP1

p-S37-GOLGA2 p-RAB1

GTP		ArrowREACT_147845 (Reactome)
p-T216,S274,S373-GORASP1

p-S37-GOLGA2 p-RAB1

GTP		REACT_147849 (Reactome)
p-T216,S274,S373-GORASP1

p-S37-GOLGA2 p-RAB1

GTP		TBarREACT_147730 (Reactome)
p-T222,225-GORASP2

BLZF1 RAB2A

GTP		ArrowREACT_147850 (Reactome)
p-T222,225-GORASP2

BLZF1 RAB2A

GTP		TBarREACT_147809 (Reactome)
p-T333-NEK9REACT_160217 (Reactome)
p-Y204-MAPK3-3/p-T185,Y187-MAPK1 homodimerREACT_147850 (Reactome)
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