Search results for PIK3C2A

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Reaction (9 results from a total of 9)

Identifier: R-HSA-8868071
Species: Homo sapiens
Compartment: plasma membrane
PIK3C2A is a member of the class II PI 3 kinases, and phosphorylates PI(4)P to PI(3,4)P2 at the plasma membrane. PIK3C2A interacts with clathrin through a clathrin-binding domain in its unique N-terminal tail and localizes to late-stage clathrin-coated pits (Domin et al, 2000; Gaidarov et al, 2001; Gaidarov et al, 2005). Binding to clathrin stimulates the kinase activity of PIK3C2A and promotes the production of PI(3,4)P2 at the plasma membrane (Gaidarov et al, 2001). PI(3,4)P2 formation by PIK3C2A contributes to maturation of clathrin-coated pits by promoting the recruitment of BAR-domain containing proteins such as SNX9, which stimulate membrane curvature required for vesicle formation and eventual fission (Posor et al, 2013; reveiwed in Daumke et al, 2014).
Identifier: R-HSA-8868072
Species: Homo sapiens
Compartment: plasma membrane
Clathrin-associated PIK3C2A catalyzes the conversion of PI(4)P to PI(3,4)P2, which contributes to the recruitment of BAR domain proteins such as SNX9 to the clathrin-coated pit (Domin et al, 2000; Gaidarov et al, 2001; Gaidarov et al, 2005; Posor et al, 2013; reviewed in Daumke et al, 2014).
Identifier: R-HSA-1676206
Species: Homo sapiens
Compartment: early endosome membrane, cytosol
At the early endosome membrane, phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit alpha (PIK3C2A) (Kraq et al. 2010, Arcaro et al. 2000) phosphorylates phosphatidylinositol 4-phosphate (PI4P) to phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2).
Identifier: R-HSA-1675961
Species: Homo sapiens
Compartment: Golgi membrane, cytosol
At the Golgi membrane, phosphatidylinositol 3-kinase catalytic subunit type 3 (PIK3C3) aka VPS34 is bound to phosphoinositide 3-kinase regulatory subunit 4 (PIK3R4). This PIK3C3:PIK2R4 complex and phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit alpha (PIK3C2A) phosphorylate phosphatidylinositol (PI) to phosphatidylinositol 3-phosphate (PI3P).

The following lists the above proteins with their corresponding literature references: PIK3C3:PIK2R4 (Panaretou et al. 1997, Volinia et al. 1995) and PIK3C2A (Arcaro et al. 2000, Domin et al. 2000).
Identifier: R-HSA-1676024
Species: Homo sapiens
Compartment: late endosome membrane, cytosol
At the late endosome membrane, phosphatidylinositol 3-kinase catalytic subunit type 3 (PIK3C3) aka VPS34 binds to phosphoinositide 3-kinase regulatory subunit 4 (PIK3R4). The PIK3C3:PIK3R4 complex and phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit alpha (PIK3C2A) phosphorylate phosphatidylinositol (PI) to phosphatidylinositol 3-phosphate (PI3P).

The following lists the above proteins with their corresponding literature references: PIK3C3:PIK3R4 (Panaretou et al. 1997, Volinia et al. 1995, Cao et al. 2007) and PIK3C2A (Arcaro et al. 2000, Domin et al. 2000).
Identifier: R-HSA-1675939
Species: Homo sapiens
Compartment: early endosome membrane, cytosol
At the early endosome membrane, phosphatidylinositol 3-kinase catalytic subunit type 3 (PIK3C3) aka VPS34 binds to phosphoinositide 3-kinase regulatory subunit 4 (PIK3R4). The PIK3C3:PIK3R4 complex and phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit alpha (PIK3C2A) phosphorylate phosphatidylinositol (PI) to phosphatidylinositol 3-phosphate (PI3P).

The following lists the above proteins with their corresponding literature references: PIK3C3:PIK3R4 complex (Panaretou et al. 1997, Volinia et al. 1995, Cao et al. 2007) and PIK3C2A (Arcaro et al. 2000, Domin et al. 2000).
Identifier: R-HSA-1675928
Species: Homo sapiens
Compartment: Golgi membrane, cytosol
At the Golgi membrane, phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit alpha (PIK3C2A) (Domin et al. 2000, Arcaro et al. 2000) and phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit gamma (PIK3C2G) (Ono et al. 1998, Rozycka et al. 1998, Misawa et al. 1998) phosphorylate phosphatidylinositol 4-phosphate (PI4P) to phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2). PIK3C2G phosphorylates phosphatidylinositol (PI) and PI4P but not phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2).
Identifier: R-HSA-1676109
Species: Homo sapiens
Compartment: plasma membrane, cytosol
At the plasma membrane, phosphatidylinositol-4,5-bisphosphate (PI(4,5)P2) 3-kinase catalytic subunits form complexes with regulatory subunits. These complexes along with phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunits alpha (PIK3C2A), beta (PIK3C2B), and gamma (PIK3C2G) phosphorylate phosphatidylinositol 4-phosphate (PI4P) to phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2). The PI(4,5)P2 3-kinase complexes involved are: PI(4,5)P2 3-kinase catalytic subunit alpha isoform (PIK3CA) bound to PI 3-kinase regulatory subunit alpha/beta/gamma (PIK3R1/2/3); beta (PIK3CB) bound to PIK3R1/2/3; delta (PIK3CD) bound to PIK3R1/2/3; and gamma (PIK3CG) bound to PI 3-kinase regulatory subunit 5 (PIK3R5) or 6 (PIK3R6).

The following lists the above proteins with their corresponding literature references: PIK3C2A (Arcaro et al. 2000); PIK3C2B (Arcaro et al. 2000, Arcaro et al. 1998); PIK3C2G (Misawa et al. 1998, Ono et al. 1998); PIK3CA:PIK3R1, PIK3CA:PIK3R2, PIK3CA:PIK3R3 (Vanhaesebroeck et al. 1997); PIK3CB:PIK3R1, PIK3CB:PIK3R2, PIK3CB:PIK3R3 (Meier et al. 2004, Guo et al. 1997); PIK3CD:PIK3R1, PIK3CD:PIK3R2, PIK3CD:PIK3R3 (Vanhaesebroeck et al. 1997); and PIK3CG:PIK3R5, PIK3CG:PIK3R6 (Suire et al. 2005, Stoyanov et al. 1995).
Identifier: R-HSA-8867754
Species: Homo sapiens
Compartment: plasma membrane
BAR (BIN/amphiphysin/Rvs) domain proteins sense and contribute to membrane curvature. BAR domain proteins generally form long, coiled-coil homo- or hetero-dimers with a concave inner surface that interacts with membranes (reviewed in Gallop and McMahon, 2005; Daumke et al, 2014). F-BAR domain proteins such as FCHo 1 and 2 recognize shallow membrane curvature and are generally recruited early in the formation of clathrin-coated pit (Itoh et al, 2005; Kamioka et al, 2004; Henne et al, 2007; Shimada et al, 2007; Henne et al, 2010). FNBP proteins and N-BAR containing endocytic proteins such as SNX9 and 18, amphiphysin (AMPH) and endophilins recognize regions of membrane with greater curvature, interact with dynamin and likely play a later role in CCP formation with spatiotemporal coupling to vesicle scission (Kamioka et al, 2004; Itoh et al, 2005; Soulet et al, 2005; Shimada et al, 2007; Shin et al, 2008; Taylor et al, 2011; reveiwed in McMahon and Boucrot, 2011). These proteins are recruited to the complex through interactions with core components of the clathrin-coated pit, and in the case of SNX9, also through interaction with PI(3,4)P2, which is generated at late stages by clathrin-associated PIK3C2A (Lundmark and Carlson, 2003; Schmid et al, 2006; Dergai et al, 2010; Brett et al, 2002 : Posor et al, 2013; reviewed in Daumke et al, 2014). Early BAR domain containing proteins such as FCHo1 and 2 are not present in either late stage clathrin-coated pits or in free clathrin-coated vesicles. Although the precise timing of their dissociation is not known, in this pathway, they are shown leaving the clathrin-coated pit upon recruitment of the more highly curved N-BAR proteins (Taylor et al, 2011).
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