Search results for VAPB

Showing 13 results out of 16

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Types

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Protein (2 results from a total of 2)

Identifier: R-HSA-429718
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane
Primary external reference: UniProt: VAPB: O95292
Identifier: R-HSA-9715115
Species: Homo sapiens
Compartment: Golgi membrane
Primary external reference: UniProt: VAPB: O95292

Reaction (10 results from a total of 13)

Identifier: R-HSA-429694
Species: Homo sapiens
Compartment: cytosol, endoplasmic reticulum membrane
CERT1-2 (ceramide transfer protein, isoform 2) can dissociate from its complex in the endoplasmic reticulum membrane with VAPA or VAPB (VAMP-associated proteins A or B) and PPM1L (protein phosphatase 1-like) and is released into the cytosol (Kawano et al. 2006; reviewed by Kumagai & Hanada, 2019).
Identifier: R-HSA-429732
Species: Homo sapiens
Compartment: cytosol, endoplasmic reticulum membrane
Multiphospho-CERT retains its affinity for VAPA or VAPB (VAMP-associated proteins A or B) and PPM1L (protein phosphatase 1-like) in the endoplasmic reticulum membrane, and can associate with them to form a membrane-associated complex (Kawano et al., 2006; Saito et al. 2008; reviewed by Kumagai & Hanada, 2019).
Identifier: R-HSA-9693250
Species: Homo sapiens
Compartment: Golgi membrane, cytosol
Active GTP bound RHOD binds the following effectors at the Golgi membrane:
FILIP1 (Gad et al. 2012)
WHAMM (Gad et al. 2012; Blom et al. 2015)

The following candidate effectors were reported to bind active RHOD by Bagci et al. 2020:
GOLGA8R (Bagci et al. 2020)
LMAN1 (Bagci et al. 2020)
VAPB (Bagci et al. 2020)
Identifier: R-HSA-9714361
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane
Based on the high throughput screen conducted by Bagci et al. 2020, constitutively active RHOC binds to the following candidate effectors, known to reside at the endoplasmic reticulum membrane:
LBR (Bagci et al. 2020)
LMAN1 (Bagci et al. 2020)
MACO1 (Bagci et al. 2020)
PGRMC2 (Bagci et al. 2020)
STX5 (Bagci et al. 2020)
VAPB (Bagci et al. 2020)
Identifier: R-HSA-9714481
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane
Active RAC2 binds the following candidate effectors at the endoplasmic reticulum membrane:
ANKLE2 (Bagci et al. 2020)
EMD (Bagci et al. 2020)
ESYT1 (Bagci et al. 2020)
LBR (Bagci et al. 2020)
LEMD3 (Bagci et al. 2020)
LMAN1 (Bagci et al. 2020)
PGRMC2 (Bagci et al. 2020)
VAPB (Bagci et al. 2020)
VRK2 (Bagci et al. 2020)
Identifier: R-HSA-429683
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane
CERT1-2 (ceramide transfer protein, isoform 2), associated with the cytosolic face of the endoplasmic reticulum (ER) in a complex with VAPA or VAPB (VAMP-associated proteins A or B) (Kawano et al. 2006) and PPM1L (protein phosphatase 1-like) (Saito et al. 2008), can bridge the gap between the ER and the Golgi apparatus via its PH domain and transfer a molecule of ceramide extracted from the ER membrane to the Golgi at the ER-Golgi membrane contact sites (MCS) (Hanada et al. 2003; Saito et al. 2008). CERT1-2-mediated ceramide transfer is positively regulated by OSBP (oxysterol binding protein), apparently through accumulation of phosphatidylinositol 4-phosphate (PI-4P) at MCS (Perry and Ridgway 2006; Goto et al., 2016). Non-vesicular transport of ceramide from endoplasmic reticulum to Golgi membranes is essential for cellular lipid homeostasis (reviewed by Olaiyoye et al., 2012; Kumagai & Hanada, 2019).
Identifier: R-HSA-429699
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane
CERT1-2 (ceramide transfer protein, isoform 2), an isoform of COL4A3BP, mediates the translocation of ceramides from the endoplasmic reticulum (ER) membrane to the membrane of the Golgi apparatus at the ER-Golgi membrane contact sites (MCS). Immunoprecipitation experiments suggest that CERT1-2 is associated with the ER membrane as part of a complex with PPM1L (protein phosphatase 1-like) (Saito et al. 2008) and VAPA or VAPB (VAMP-associated proteins A or B) (Kawano et al. 2006). The carboxyterminal START domain of CERT1-2 protein specifically binds ceramides (Hanada et al. 2003; Kudo et al. 2008). Non-vesicular transport of ceramide from endoplasmic reticulum to Golgi membranes is essential for cellular lipid homeostasis (reviewed by Olaiyoye et al., 2012; Kumagai & Hanada, 2019). While there is no direct support for the transfer of other ceramides than Cer(d18:1/16:0), it makes sense to assume other ceramides are transported, as well.
Identifier: R-HSA-9014467
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane
Active GTP-bound RHOG binds to and activates kinectin (KTN1) at the endoplasmic reticulum membrane (Vignal et al. 2001).

In addition, active RHOG binds to the following candidate endoplasmic reticulum membrane effectors identified in the high throughput screen by Bagci et al. 2020:
ANKLE2 (Bagci et al. 2020)
EMD (Bagci et al. 2020)
ESYT1 (Bagci et al. 2020)
LBR (Bagci et al. 2020)
LEMD3 (Bagci et al. 2020)
LETM1 (Bagci et al. 2020)
LMAN1 (Bagci et al. 2020)
NDUFA5 (Bagci et al. 2020)
PGRMC2 (Bagci et al. 2020)
STX5 (Bagci et al. 2020)
VAPB (Bagci et al. 2020)
VRK2 (Bagci et al. 2020)
YKT6 (Bagci et al. 2020)
Identifier: R-HSA-9013004
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane
Kinectin, a kinesin anchor involved in kinesin mediated vesicle motility, interacts with the GTP bound (active) form of RHOA (Hotta et al. 1996, Alberts et al. 1998, Vignal et al. 2001).

The following endoplasmic reticulum proteins have been identified as putative RHOA effectors in the high throughput screen by Bagci et al. and are annotated as candidate RHOA effectors:
ATP6AP1 (Bagci et al. 2020)
BCAP31 (Bagci et al. 2020)
CCDC115 (Bagci et al. 2020)
DDRGK1 (Bagci et al. 2020)
EMC3 (Bagci et al. 2020)
LBR (Bagci et al. 2020)
LMAN1 (Bagci et al. 2020)
MACO1 (Bagci et al. 2020)
PGRMC2 (Bagci et al. 2020)
STX5 (Bagci et al. 2020)
TEX2 (Bagci et al. 2020)
TMEM87A (Bagci et al. 2020)
VAPB (Bagci et al. 2020)
YKT6 (Bagci et al. 2020)
Identifier: R-HSA-9693125
Species: Homo sapiens
Compartment: plasma membrane, cytosol
Active GTP-bound RHOF binds the following effectors:
BAIAP2L1 (Sudhaharan et al. 2016)
BAIAP2L2 (Sudhaharan et al. 2016)
DIAPH1 (Fan et al. 2010)
DIAPH2 (Gorelik et al. 2011)
FARP1 (Fan et al. 2015)

The following candidate RHOF effectors that can localize to cytosol or the plasma membrane were reported by Bagci et al. 2020 to bind active RHOF:
ACTB (Bagci et al. 2020)
ACTN1 (Bagci et al. 2020)
ADD3 (Bagci et al. 2020)
AKAP12 (Bagci et al. 2020)
ARHGAP1 (Bagci et al. 2020)
ARHGAP39 (Bagci et al. 2020)
BASP1 (Bagci et al. 2020)
CAPZB (Bagci et al. 2020)
CAV1 (Bagci et al. 2020)
CPNE8 (Bagci et al. 2020)
DIAPH3 (Bagci et al. 2020)
ESYT1 (Bagci et al. 2020)
FAM169A (Bagci et al. 2020)
LMNB1 (Bagci et al. 2020)
MCAM (Bagci et al. 2020)
MTMR1 (Bagci et al. 2020)
POTEE (Bagci et al. 2020)
RAB7A (Bagci et al. 2020)
SENP1 (Bagci et al. 2020)
SLC4A7 (Bagci et al. 2020)
SNAP23 (Bagci et al. 2020)
SOWAHC (Bagci et al. 2020)
STEAP3 (Bagci et al. 2020)
TMPO (Bagci et al. 2020)
TOR1AIP1 (Bagci et al. 2020)
VAMP3 (Bagci et al. 2020)
VANGL1 (Bagci et al. 2020)

Several putative effectors that localize to endoplasmic reticulum, endosomes or the mitochondrial outer membrane were reported to bind active RHOF by Bagci et al. 2020, but as the localization of RHOF to these cellular compartments has not been established, these effectors have not been annotated:
EMD
LBR
LEMD3
LMAN1
PGRMC2
VRK2

The following putative effectors were reported not to bind active RHOF:
DBN1 (Bagci et al. 2020)
EFHD2 (Bagci et al. 2020)
GOLGA8R (Bagci et al. 2020)
HINT2 (Bagci et al. 2020)
MOSPD2 (Bagci et al. 2020)
STBD1 (Bagci et al. 2020)
VAPB (Bagci et al. 2020)

Pathway (1 results from a total of 1)

Identifier: R-HSA-428157
Species: Homo sapiens
Sphingolipids are derivatives of long chain sphingoid bases such as sphingosine (trans-1,3-dihydroxy 2-amino-4-octadecene), an 18-carbon unsaturated amino alcohol which is the most abundant sphingoid base in mammals. Amide linkage of a fatty acid to sphingosine yields ceramides. Esterification of phosphocholine to ceramides yields sphingomyelin, and ceramide glycosylation yields glycosylceramides. Introduction of sialic acid residues yields gangliosides. These molecules appear to be essential components of cell membranes, and intermediates in the pathways of sphingolipid synthesis and breakdown modulate processes including apoptosis and T cell trafficking.

While sphingolipids are abundant in a wide variety of foodstuffs, these dietary molecules are mostly degraded by the intestinal flora and intestinal enzymes. The body primarily depends on de novo synthesis for its sphingolipid supply (Hannun and Obeid 2008; Merrill 2002). De novo synthesis proceeds in four steps: the condensation of palmitoyl-CoA and serine to form 3-ketosphinganine, the reduction of 3-ketosphinganine to sphinganine, the acylation of sphinganine with a long-chain fatty acyl CoA to form dihydroceramide, and the desaturation of dihydroceramide to form ceramide.

Other sphingolipids involved in signaling are derived from ceramide and its biosynthetic intermediates. These include sphinganine (dihydrosphingosine) 1-phosphate, phytoceramide, sphingosine, and sphingosine 1-phosphate.

Sphingomyelin is synthesized in a single step in the membrane of the Golgi apparatus from ceramides generated in the endoplasmic reticulum (ER) membrane and transferred to the Golgi by CERT (ceramide transfer protein), an isoform of COL4A3BP that is associated with the ER membrane as a complex with PPM1L (protein phosphatase 1-like) and VAPA or VAPB (VAMP-associated proteins A or B). Sphingomyelin synthesis appears to be regulated primarily at the level of this transport process through the reversible phosphorylation of CERT (Saito et al. 2008).

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