Search results for GAK

Showing 12 results out of 12

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Species

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Protein (3 results from a total of 3)

GAK

Identifier: R-HSA-434203
Species: Homo sapiens
Compartment: cytoplasmic vesicle membrane
Primary external reference: UniProt: GAK: O14976

GAK

Identifier: R-HSA-434340
Species: Homo sapiens
Compartment: Golgi membrane
Primary external reference: UniProt: GAK: O14976

GAK

Identifier: R-HSA-8868619
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: GAK: O14976

Set (1 results from a total of 1)

Identifier: R-HSA-8868618
Species: Homo sapiens
Compartment: cytosol

Complex (2 results from a total of 2)

Identifier: R-HSA-6810024
Species: Homo sapiens
Compartment: cytosol
Identifier: R-NUL-6810029
Species: Mus musculus, Homo sapiens
Compartment: cytosol

Reaction (6 results from a total of 6)

Identifier: R-HSA-6810030
Species: Homo sapiens
Compartment: cytosol
Based on a high throughput study of human interactome in HeLa cells, MTMR2 forms a complex with MTMR10, an enzymatically inactive myotubularin family member. The function of this complex has not been examined (Hein et al. 2015).
Identifier: R-NUL-6810026
Species: Mus musculus, Homo sapiens
Compartment: cytosol
Based on a high throughput study of human interactome in HeLa cells stably expressing tagged mouse Mtmr2 (97% identical to human MTMR2) under the control of mouse Mtmr2 promoter, Mtmr2 forms a complex with endogenous human MTMR10 (Hein et al. 2015).
Identifier: R-HSA-432688
Species: Homo sapiens
Compartment: cytosol
The heat shock protein Hsc70 and auxilin, a J-domain containing protein, are responsible for clathrin disassembly through an ATP-dependent reaction. This uncoating step may be a point in the pathway subject to regulation. This final step releases the vesicle from the clathrin cage. The vesicle still contatins a specific Vamp molecule, part of the targeting and fusion mechanism that delivers the vesicle to its ultimate destination. This vesicle also contains its cargo, membrane proteins embeded in the lysosome membrane.
Identifier: R-HSA-421836
Species: Homo sapiens
Compartment: cytosol
The heat shock protein Hsc70 and auxilin, a J-domain containing protein, are responsible for clathrin disassembly through an ATP-dependent reaction. This uncoating step may be a point in the pathway subject to regulation. This final step releases the vesicle from the clathrin cage. The vesicle still contatins a specific Vamp molecule, part of the targeting and fusion mechanism that delivers the vesicle to its ultimate destination. This vesicle also contains its cargo, membrane proteins embeded in the Golgi-associated vesicle membrane.
Identifier: R-HSA-8868660
Species: Homo sapiens
Compartment: clathrin-coated endocytic vesicle membrane
HSPA8 (also known as HSC70) is recruited to the clathrin-coated vesicle through interaction with DNA J proteins GAK and DNAJC6 (Rapoport et al, 2008; Xing et al, 2010; reviewed in Sousa and Lafer, 2015). Recent studies examining the stoichiometry of uncoating predict between one and three HSPA8 molecules are required per clathrin triskelion for maximal uncoating in vitro (Bocking et al, 2011; Rothnie et al, 2011). After ATP hydrolysis, HSPA8 remains associated with the liberated clathrin, which prevents aberrant repolymerization and association of clathrin (Schlossman et al, 1984; reviewed in Sousa and Lafer, 2015).
Identifier: R-HSA-8868659
Species: Homo sapiens
Compartment: clathrin-coated endocytic vesicle membrane
After fission from the plasma membrane, auxilin proteins DNAJC6 and GAK are recruited to the vesicle through interaction with clathrin and phosphoinositides, in particular PI4P (Greener et al, 2000; Lee et al, 2006; Massol et al, 2006; Taylor et al, 2011; Scheele et al, 2001; Fotin et al, 2004a; Fotin et al, 2004b; Guan et al, 2010; reviewed in McMahon and Boucrot, 2011; Sousa and Lafer, 2015). Auxilin in turn recruits the ATPase HSPA8 (also known as HSC70) , which uses the energy from ATP hydrolysis to remove the clathrin-coat from the vesicle, priming it for fusion with a subsequent endosomal compartment (Schlossman et al, 1984; Ungewickell et al, 1995; Rappoport et al, 2008; Xing et al, 2010; Bocking et al, 2011; Rothnie et al, 2011; reviewed in McMahon and Boucrot, 2011; Sousa and Lafer, 2015).
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