Search results for RAB2A

Showing 8 results out of 8

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Protein (3 results from a total of 3)

Identifier: R-HSA-2422386
Species: Homo sapiens
Compartment: Golgi membrane
Primary external reference: UniProt: RAB2A: P61019
Identifier: R-HSA-8873716
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: RAB2A: P61019
Identifier: R-HSA-8873963
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P61019

Complex (3 results from a total of 3)

Identifier: R-HSA-2422449
Species: Homo sapiens
Compartment: Golgi membrane
Identifier: R-HSA-2422429
Species: Homo sapiens
Compartment: Golgi membrane
Identifier: R-HSA-2422951
Species: Homo sapiens
Compartment: Golgi membrane

Reaction (1 results from a total of 1)

Identifier: R-HSA-2422927
Species: Homo sapiens
Compartment: Golgi membrane, cytosol
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).

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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