Search results for RAB11A

Showing 19 results out of 19

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Protein (4 results from a total of 4)

Identifier: R-HSA-5623395
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: RAB11A: P62491
Identifier: R-HSA-2029023
Species: Homo sapiens
Compartment: recycling endosome membrane
Primary external reference: UniProt: RAB11A: P62491
Identifier: R-HSA-1458519
Species: Homo sapiens
Compartment: cytoplasmic vesicle membrane
Primary external reference: UniProt: RAB11A: P62491
Identifier: R-HSA-8873781
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: RAB11A: P62491

Complex (7 results from a total of 7)

Identifier: R-HSA-2028701
Species: Homo sapiens
Compartment: cytoplasmic vesicle membrane
Identifier: R-HSA-5623431
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-1458542
Species: Homo sapiens
Compartment: cytoplasmic vesicle membrane
Identifier: R-HSA-5637979
Species: Homo sapiens
Compartment: Golgi-associated vesicle membrane
Identifier: R-HSA-5623437
Species: Homo sapiens
Compartment: Golgi membrane
Identifier: R-HSA-5623438
Species: Homo sapiens
Compartment: Golgi-associated vesicle membrane
Identifier: R-HSA-5623434
Species: Homo sapiens
Compartment: Golgi membrane

Reaction (7 results from a total of 7)

Identifier: R-HSA-5638014
Species: Homo sapiens
Compartment: Golgi-associated vesicle membrane
The RAB8 guanine nucleotide exchange factor RAB3IP/RABIN8 is recruited to vesicles through interaction with membrane-tethered RAB11:GTP (Westlake et al, 2011; Knodler et al, 2010). Recruitment of RAB3IP may also depend on the TRAPPCII complex, a multiprotein complex with roles in vesicular trafficking (Westlake et al, 2011; reviewed in Sacher et al, 2008). RAB3IP is required for RAB8A to localize to the cilium, and depletion of RAB3IP compromises cilia formation (Nachury et al, 2007; Loktev et al, 2008). GTP-bound RAB8A may promote ciliogenesis by promoting the traffic of post-Golgi vesicles to the base of the cilium (Nachury et al, 2007; Westlake et al, 2011; Feng et al, 2012; reviewed in Reiter et al, 2012)
Identifier: R-HSA-8863973
Species: Homo sapiens
Compartment: phagocytic vesicle membrane, recycling endosome membrane
Recycling endosome-localized R-SNARE protein like RAB11a, VAMP3, and VAMP8 dock with target phagosome membrane Q-SNARE protein SNAP23. MHC-I present on the recycling endosomes would be delivered to phagosomes during this process.
Identifier: R-HSA-8863895
Species: Homo sapiens
Compartment: phagocytic vesicle membrane, cytosol
A major reserve of MHC-I in dendritic cells reside within the endocytic recycling compartments (ERC). MHC-I trafficking to the ERC is regulated by the activity of Rab11a and subsequent trafficking from ERC to phagosomes is controlled by TLR-MyD88-IKK2-dependent phosphorylation of phagosomal SNAP23. Toll-like receptor (TLR) signalling regulate cross-presentation as they regulate phagocytosis and phagolysosomal fusion (Nair et al. 2011). MHC-I bearing ERC are enriched with R-SNAREs like RAB11a, VAMP3, and VAMP8. These SNARE molecules can interact with Q-SNARE SNAP23 present on phagosomes and this mediates membrane fusion. This interaction of SNAP23 with R-SNAREs require phosphorylation of SNAP23 (on Ser-95) by IKK2, and IKK2 is activated by TLR signalling. SNAP23 phosphorylation may increase SNAP23 binding to SNAREs. It may also regulate platelet and mast cell secretion (Karim et al. 2013, Suziki & Verma 2008).
Identifier: R-HSA-5623519
Species: Homo sapiens
Compartment: Golgi membrane
RAB8A is another small GTPase that is required for ciliogenesis. RAB8A is recruited to the ciliary targeting complex at the trans-Golgi network (TGN) through interactions of the RAB8A guanine nucleotide exchange factor (GEF) RAB3IP (also known as RABIN8) with ASAP1 and RAB11 (Wang et al, 2012; Westlake et al, 2011; Feng et al, 2012; reviewed in Deretic, 2013). RAB8A is recruited in the inactive GDP bound form, and is activated at the TGN by RAB3IP in a RAB11A-dependent fashion (Hatulla et al, 2002; Knodler et al, 2010; Westlake et al, 2012; Wang et al, 2012; Feng et al, 2012).
Identifier: R-HSA-5620921
Species: Homo sapiens
Compartment: Golgi membrane
Recruitment of ASAP1 to the TGN facilitates the subsequent recruitment of both RAB11A and the RAB11 effector protein FIP3 to the ciliary targeting complex. RAB11FIP3 functions as a homodimer and can bind simultaneously to RAB11 and ARF4 through its C-terminal region (Inoue et al, 2008; Mazelova et al, 2009; Wang et al, 2012; Shiba et al, 2006; Eathiraj et al, 2006; Schonteich et al, 2007). RAB11FIP3 also interacts with the BAR domain of ASAP1 and in this way may play a role in stimulating the ARF GAP activity of ASAP1, promoting the inactivation ARF4 and its subsequent dissociation from the TGN (Inoue et al, 2008; reviewed in Deretic, 2013).
Identifier: R-HSA-8863914
Species: Homo sapiens
Compartment: endoplasmic reticulum-Golgi intermediate compartment membrane, endoplasmic reticulum membrane, integral component of lumenal side of endoplasmic reticulum membrane
In DCs subset of ER proteins including MHC-I peptide loading complex (PLC) and transporter associated with antigen processing (TAP) transit to phagosomes via the intermediate compartment ER-Golgi intermediate compartment (ERGIC) (Cebrian et al. 2011). TAP exits the ER in COPII vesicles in association with MHC class I, and that peptide translocation by TAP and binding to class I can occur in post-ER compartments (Ghanem et al. 2010). SEC22B, an ER-resident SNARE is required for the transport of PLC from ERGIC (Cebrian et al. 2011), but this step does not deliver MHC-I (Nair-Gupta et al. 2014). Instead, MHC-I are recruited from an endosomal recycling compartment (ERC), which is marked by Rab11a, VAMP3/cellubrevin, and VAMP8/endobrevin that holds large reserves of MHC-I. This step is dependent on TLR signalling (Nair-Gupta et al. 2014).
Identifier: R-HSA-2316352
Species: Homo sapiens
Compartment: cytoplasmic vesicle membrane, plasma membrane
As inferred from mouse, GLUT4 (SLC2A4) initially translocates from endosomes to insulin-responsive vesicles (IRVs, GSVs). RAB11 appears to play a role in this process. IRVs bearing GLUT4 are then translocated across the cortical actin network to the plasma membrane. Unconventional myosin 5A (MYO5A) interacts with RAB10 or RAB8A on the vesicle and participates in transport of the IRV. Myosin 1C appears to act close to the plasma membrane and may facilitate fusion of the vesicle with the plasma membrane. RAB:GTP complexes coupled to the vesicles may interact with myosins to regulate their activity. Non-muscle myosin IIA (MYH9) appears to interact with the SNAP23 complex to dock the IRV at the inner membrane face.
As inferred from mouse (Zeigerer et al. 2002) and rat (Uhlig et al. 2005), RAB11A enhances translocation of GLUT4 to the plasma membrane by mobilizing GLUT4 (SLC2A4) from endosomes to insulin responsive vesicles.
As inferred from mouse (Sano et al. 2007) and rat (Ishikura et al. 2007, Ishikura and Klip 2008, Sun et al. 2010), RAB:GTP activates translocation of GLUT4 (SLC2A4) to the plasma membrane, possibly by interacting with myosins. RAB8A, RAB10, and RAB14 predominate in 3T3-L1 adipocytes; RAB13 predominates in L6 muscle cells.
As inferred from mouse, TC10 participates in the translocation and docking of GLUT4 (SLC2A4) vesicles at the plasma membrane (Chang et al. 2007).
As inferred from mouse (Ueda et al. 2008, Ueda et al. 2010) and rat (Chiu et al. 2010), RAC1:GTP enhances translocation of GLUT4 (SLC2A4) to the plasma membrane by causing actin remodeling that requires ARP2/3. The exact mechanism of RAC1 action is unknown.

Pathway (1 results from a total of 1)

Identifier: R-HSA-5620920
Species: Homo sapiens
Proteomic studies suggest that the cilium is home to approximately a thousand proteins, and has a unique protein and lipid make up relative to the bulk cytoplasm and plasma membrane (Pazour et al, 2005; Ishikawa et al, 2012; Ostrowoski et al, 2002; reviewed in Emmer et al, 2010; Rohatgi and Snell, 2010). In addition, the cilium is a dynamic structure, and the axoneme is continually being remodeled by addition and removal of tubulin at the distal tip (Marshall and Rosenbaum, 2001; Stephens, 1997; Song et al, 2001). As a result, the function and structure of this organelle relies on the directed trafficking of protein and vesicles to the cilium. Small GTPases of the RAS, RAB, ARF and ARL families are involved in cytoskeletal organization and membrane traffic and are required to regulate the traffic from the Golgi and the trans-Golgi network to the cilium (reviewed in Deretic, 2013; Li et al, 2012). ARF4 is a Golgi-resident GTPase that acts in conjunction with a ciliary-targeting complex consisting of the ARF-GAP ASAP1, RAB11A, the RAB11 effector FIP3 and the RAB8A guanine nucleotide exchange factor RAB3IP/RABIN8 to target cargo bearing a putative C-terminal VxPx targeting motif to the cilium. A well-studied example of this system involves the trafficking of rhodopsin to the retinal rod photoreceptors, a specialized form of the cilium (reviewed in Deretic, 2013). ARL3, ARL13B and ARL6 are all small ARF-like GTPases with assorted roles in ciliary trafficking and maintenance. Studies in C. elegans suggest that ARL3 and ARL13B have opposing roles in maintaining the stability of the anterograde IFT trains in the cilium (Li et al, 2010). In addition, both ARL3 and ARL13B have roles in facilitating the traffic of subsets of ciliary cargo to the cilium. Myristoylated cargo such as peripheral membrane protein Nephrocystin-3 (NPHP3) is targeted to the cilium in a UNC119- and ARL3-dependent manner, while ARL13B is required for the PDE6-dependent ciliary localization of INPP5E (Wright et al, 2011; Humbert et al, 2012; reviewed in Li et al, 2012). ARL6 was also identified as BBS3, a gene that when mutated gives rise to the ciliopathy Bardet-Biedl syndrome (BBS). ARL6 acts upstream of a complex of 8 other BBS-associated proteins known as the BBSome. ARL6 and the BBSome are required for the ciliary targeting of proteins including the melanin concentrating hormone receptor (MCHR) and the somatostatin receptor (SSTR3), among others (Nachury et al, 2007; Loktev et al, 2008; Jin et al, 2010; Zhang et al, 2011). Both the BBSome and ARL6 may continue to be associated with cargo inside the cilium, as they are observed to undergo typical IFT movements along the axoneme (Fan et al, 2004; Lechtreck et al, 2009; reviewed in Li et al, 2012).
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