Search results for GORASP1

Showing 19 results out of 27

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Protein (4 results from a total of 4)

Identifier: R-HSA-162984
Species: Homo sapiens
Compartment: endoplasmic reticulum-Golgi intermediate compartment membrane
Primary external reference: UniProt: GORASP1: Q9BQQ3
Identifier: R-HSA-6808767
Species: Homo sapiens
Compartment: Golgi membrane
Primary external reference: UniProt: GORASP1: Q9BQQ3
Identifier: R-HSA-2172182
Species: Homo sapiens
Compartment: Golgi membrane
Primary external reference: UniProt: GORASP1: Q9BQQ3
Identifier: R-HSA-2314415
Species: Homo sapiens
Compartment: Golgi membrane
Primary external reference: UniProt: GORASP1: Q9BQQ3

Reaction (7 results from a total of 9)

Identifier: R-HSA-2214351
Species: Homo sapiens
Compartment: Golgi membrane, cytosol
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).
Identifier: R-NUL-2423781
Species: Rattus norvegicus, Homo sapiens
Compartment: Golgi membrane
Human PLK1 from HeLa cell extracts binds recombinant rat Gorasp1 that was previously phosphorylated by CDK1 (Preisinger et al. 2005).
Identifier: R-HSA-2172194
Species: Homo sapiens
Compartment: Golgi membrane, cytosol
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).
Identifier: R-HSA-2314566
Species: Homo sapiens
Compartment: Golgi membrane
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).
Identifier: R-HSA-2172183
Species: Homo sapiens
Compartment: Golgi membrane, cytosol
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).
Identifier: R-NUL-2422970
Species: Rattus norvegicus, Homo sapiens
Compartment: Golgi membrane, cytosol
The existence of Gorasp1:Golga2:Uso1:Rab1:GTP complex was established by co-immunoprecipitation of exogenously expressed human RAB1A (identical sequence to rat Rab1A) from normal rat kidney cells, NRKs (Moyer et al. 2001). It was also shown that human RAB1B binds human GM130 (Weide et al. 2001). In mitotic prophase, human 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), was shown to phosphorylate recombinant rat Gorasp1 and Golga2, as well as RAB1A (Bailly et al. 1991, Lowe et al. 1998, Preisinger et al. 2005) . Phosphorylation of Golga2 and RAB1A impairs their association with Uso1 (Lowe et al. 1998, Seeman et al. 2000, Moyer et al. 2001).
Identifier: R-HSA-5694418
Species: Homo sapiens
Compartment: Golgi membrane
Protein protein interactions involving activated RAB1:GTP help dock the ER-derived vesicle on the cis-Golgi membrane (reviewed in Lord et al, 2013) . Independently, RAB:GTP interacts with both the USO1 homodimer (a long coiled coil tethering factor also known as p115) and the GOLGA2 component of the GOLGA2:GORASP1 complex on the cis-Golgi membrane (Allan et al, 2000; Moyer et al, 2001; Weide et al, 2001). USO1 also contacts GOLGA2 directly (Nakamura et al, 1997; Seeman et al, 2000). t-SNARES such as STX5, GOSR1and GOSR2 also participate in this complex on the cis-ERGIC membrane (Brandon et al, 2006; Shorter et al, 2002; reviewed in Brandizzi and Barlowe, 2013).

Complex (7 results from a total of 13)

Identifier: R-HSA-6808820
Species: Homo sapiens
Compartment: Golgi membrane
Identifier: R-HSA-5694327
Species: Homo sapiens
Compartment: endoplasmic reticulum-Golgi intermediate compartment membrane
Identifier: R-NUL-2423779
Species: Rattus norvegicus, Homo sapiens
Compartment: Golgi membrane
Identifier: R-HSA-5694326
Species: Homo sapiens
Compartment: endoplasmic reticulum-Golgi intermediate compartment membrane
Identifier: R-HSA-2172177
Species: Homo sapiens
Compartment: Golgi membrane
Identifier: R-NUL-2422980
Species: Rattus norvegicus, Homo sapiens
Compartment: Golgi membrane
Identifier: R-NUL-2422975
Species: Rattus norvegicus, Homo sapiens
Compartment: Golgi membrane

Pathway (1 results from a total of 1)

Identifier: R-HSA-162658
Species: Homo sapiens
Compartment: Golgi membrane, ER to Golgi transport vesicle membrane, cytosol
The pericentriolar stacks of Golgi cisternae undergo extensive fragmentation and reorganization in mitosis.

In mammalian cells, Golgi apparatus consists of stacked cisternae that are connected by tubules to form a ribbon-like structure in the perinuclear region, in vicinity of the centrosome. Reorganization of the Golgi apparatus during cell division allows both daughter cells to inherit this organelle, and may play additional roles in the organization of the mitotic spindle.

First changes in the structure of the Golgi apparatus likely start in G2 and are subtle, involving unlinking of the Golgi ribbon into separate stacks. These changes are required for the entry of mammalian cells into mitosis (Sutterlin et al. 2002). This initial unlinking of the Golgi ribbon depends on GRASP proteins and on CTBP1 (BARS) protein, which induces the cleavage of the tubular membranes connecting the stacks (Hidalgo Carcedo et al. 2004, Colanzi et al. 2007), but the exact mechanism is not known. Activation of MEK1/2 also contributes to unlinking of the Golgi ribbon in G2 (Feinstein and Linstedt 2007).

From prophase to metaphase, Golgi cisternae undergo extensive fragmentation that is a consequence of unstacking of Golgi cisternae and cessation of transport through Golgi. At least three mitotic kinases, CDK1, PLK1 and MEK1, regulate these changes. CDK1 in complex with cyclin B phosphorylates GOLGA2 (GM130) and GORASP1 (GRASP65), constituents of a cis-Golgi membrane complex (Lowe et al. 1998, Preisinger et al. 2005). Phosphorylation of GOLGA2 prevents binding of USO1 (p115), a protein localizing to the membrane of ER (endoplasmic reticulum) to Golgi transport vesicles and cis-Golgi, thereby impairing fusion of these vesicles with cis-Golgi cisternae and stopping ER to Golgi transport (Lowe et al. 1998, Seeman et al. 2000, Moyer et al. 2001). Phosphorylation of GORASP1 by CDK1 enables further phosphorylation of GORASP1 by PLK1 (Sutterlin et al. 2001, Preisinger et al. 2005). Phosphorylation of GORASP1 by CDK1 and PLK1 impairs stacking of Golgi cisternae by interfering with formation of GORASP1 trans-oligomers that would normally link the Golgi cisternae together (Wang et al. 2003, Wang et al. 2005, Sengupta and Linstedt 2010).

In the median Golgi, GORASP2 (GRASP55), a protein that forms a complex with BLFZ1 (Golgin-45) and RAB2A GTPase and contributes to cisternae stacking and Golgi trafficking (Short et al. 2001), is also phosphorylated in mitosis. Phosphorylation of GORASP2 by MEK1/2-activated MAPK1 (ERK2) and/or MAPK3-3 (ERK1b in human, Erk1c in rat) contributes to Golgi unlinking in G2 and fragmentation of Golgi cisternae in mitotic prophase (Acharya et al. 1998, Jesch et al. 2001, Colanzi et al. 2003, Shaul and Seger 2006, Duran et al. 2008, Feinstein and Linstedt 2007, Feinstein and Linstedt 2008, Xiang and Wang 2010).
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