Search results for RAF1

Showing 26 results out of 174

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Types

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Protein (5 results from a total of 71)

Identifier: R-HSA-167205
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P04049
Identifier: R-HSA-5675193
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: RAF1: P04049
Identifier: R-HSA-5672664
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: RAF1: P04049
Identifier: R-HSA-5624469
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: RAF1: P04049
Identifier: R-HSA-5675420
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: P04049

Set (5 results from a total of 9)

Identifier: R-HSA-9656167
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-9656165
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-9656152
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-9656156
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-9656161
Species: Homo sapiens
Compartment: cytosol

Reaction (5 results from a total of 50)

Identifier: R-HSA-9656212
Species: Homo sapiens
Compartment: plasma membrane
RAF1 mutants in cancer and germline disorders such as Noonan syndrome undergo enhanced dimerization and activation with BRAF, leading to high levels of downstream signaling. This has been observed even in cases of RAF1 mutations with abrogated or impaired kinase activity (Razzaque et al, 2007; Pandit et al, 2007; Kobayashi et al, 2010; Wu et al, 2012; Krauthammer et al, 2015; reviewed in Rauen, 2013).
Identifier: R-HSA-5675194
Species: Homo sapiens
Compartment: plasma membrane
RAF1 is phosphorylated by activated MAPK at 6 serine residues (S29, S43, S289, S296, S301 and S642). MAPK-dependent hyperphosphorylation of RAF1 abrogates the ability of activated RAF1 to interact with RAS and is coincident with inactivation of RAF1. RAF1 proteins containing mutation of these phosphorylation sites persist at the plasma membrane, show sustained S338 phosphorylation and persistent activation relative to WT RAF1 protein. In wild type cells, PP2A and the prolyl-isomerase PIN1 contribute to the dephosphorylation of hyperphosphorylated RAF1, allowing subsequent cycles of activation to occur (Dougherty et al, 2005; reviewed in Roskoski, 2010)
Identifier: R-HSA-443831
Species: Homo sapiens
Compartment: cytosol
14-3-3 family proteins can bind Raf1 and have been suggested to activate Raf1, but this has been refuted.
Identifier: R-HSA-5675431
Species: Homo sapiens
Compartment: plasma membrane
Along with PPP5C-mediated dephophosphorylation of the NtA region, PP2A contributes to the inactivation of RAF1 by mediating the dephosphorylation of AL loop residues. PP2A-mediated dephosphorylation of RAF1 may be stimulated by the prior hyperphosphorylation of RAF1 by MAPKs (Dougherty et al, 2005; reviewed in Matallanas et al, 2011).
Identifier: R-HSA-5624494
Species: Homo sapiens
Compartment: plasma membrane, cytosol
Upon CLEC7A (Dectin-1) and CD209 (DC-SIGN) activation, RAF1 translocates to the membrane through interaction with the active form of RAS. This interaction induces a conformational change in RAF1 and is required for RAF1 activation (Gringhuis et al. 2007, Wellbrock et al. 2004).

Pathway (5 results from a total of 10)

Identifier: R-HSA-9656223
Species: Homo sapiens
RAF1, also known as CRAF, is mutated in a number of germline RASopathies including Noonan Syndrome, Costello Syndrome and others, and also at low frequency in a number of cancers (reviewed in Rauen, 2013; Samatar and Poulikakos, 2015). Activating mutations cluster around conserved region 2 (CR2) which is required for regulation of the protein and the activation segment in CR3 (reviewed in Rauen, 2013).
Identifier: R-HSA-9027284
Species: Homo sapiens
The RAS guanine nucleotide exchange factors SOS1 and VAV1 bind indirectly to the phosphorylated EPOR via CRKL, SHC1, and GRB2 (Miura et al. 1994, Hanazono et al. 1996, Odai et al. 1997, Arai et al. 2001, reviewed in Kuhrt et al. 2015) . The phosphorylated cytoplasmic domain of EPOR binds CRKL, which is then phosphorylated (Arai et al. 2001). Phosphorylated CRKL binds SHC1, which is then phosphorylated and binds either GRB2:SOS1 (Barber et al. 1997) or GRB2:VAV1 (Hanazono et al. 1996). SOS1 and phosphorylated VAV1 catalyze the exchange of GDP for GTP bound to RAS, that is, RAS:GDP is converted to RAS:GTP.
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).
Identifier: R-HSA-1839120
Species: Homo sapiens
Compartment: cytosol, extracellular region, plasma membrane, nucleoplasm
Amplification or activation of FGFR1 has been reported in lung cancer (Weiss, 2001; Marek, 2009; Dutt, 2011), breast cancer (Reis-Filho, 2006; Turner, 2010), oral squamous carcinoma (Freier, 2007), esophageal squamous cell carcinomas (Ishizuka, 2002), ovarian cancer (Gorringe, 2007), bladder cancer (Simon, 2001), prostate cancer (Edwards, 2003; Acevedo, 2007) and rhabodomyosarcoma (Missiaglia, 2009). Unlike the case for FGFR2 amplifications, FGFR1 amplifications are not associated with additional point mutations and affect signaling without altering the intrinsic kinase activity of the receptor. Overexpressed FGFR1 appears to signal at a basal level in a ligand-independent fashion, but is also able to be stimulated by exogenous ligand. Downstream activation may be the result of aberrant paracrine or autocrine stimulation (reviewed in Turner and Gross, 2010; Greulich and Pollock, 2011). FGFR1 amplification has not been conclusively demonstrated to be the causative oncogenic agent in all of the cancer types mentioned above, and other genes in the 8p11 region may also be candidates in some cases (Bass, 2009; Bernard-Pierrot, 2008; Ray, 2004).
Identifier: R-HSA-5674499
Species: Homo sapiens
MAPK pathway activation is limited by a number of negative feedback loops established by MAPK-dependent phosphorylations. Known substrates of activated MAPK proteins that lie upstream in the RAF/MAPK pathway include SOS, RAF1, BRAF, and MAP2K1 (Buday et al, 1995; Dong et al, 1996; Dougherty et al, 2005; Sturm et al, 2010; Fritsche-Guenther et al, 2011; Rushworth et al, 2006; Brummer et al, 2003; Ritt et al, 2010; Catalanotti et al, 2009)

Complex (5 results from a total of 33)

Identifier: R-HSA-5675414
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-5675430
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-9656179
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-5675413
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-5675412
Species: Homo sapiens
Compartment: plasma membrane

Icon (1 results from a total of 1)

Species: Homo sapiens
Curator: Steve Jupe
Designer: Cristoffer Sevilla
ARAF,BRAF,RAF1 icon
Set of Serine/threonine-protein kinase A-Raf, Serine/threonine-protein kinase B-raf and RAF proto-oncogene serine/threonine-protein kinase
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