Search results for UNC119

Showing 12 results out of 14

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Interactor (1 results from a total of 1)

Identifier: Q13432
Species: Homo sapiens
Primary external reference: UniProt: Q13432

Protein (2 results from a total of 2)

Identifier: R-HSA-5618271
Species: Homo sapiens
Compartment: cilium
Primary external reference: UniProt: UNC119B: A6NIH7
Identifier: R-HSA-5624097
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: A6NIH7

Reaction (6 results from a total of 8)

Identifier: R-HSA-5624131
Species: Homo sapiens
Compartment: cytosol
UNC119B is an ARL3 effector that binds directly to the myristoyl moieties at glycine 2 of NPHP3 and CYS1 (Wright et al, 2011). Myristoylation is required for the ciliary localization of these proteins (Wright et al, 2011; Tao et al, 2006), and both mutation of the glycine 2 myristoylation target in NPHP3 and siRNA knockdown of UNC119B dramatically reduce the ciliary localization of NPHP3 and CYS1 (Tao et al, 2006; Wright et al, 2011; reviewed in Schwarz et al, 2012).
Identifier: R-HSA-5624133
Species: Homo sapiens
Compartment: cilium
ARL3 is an ARF-like small GTPase that is localized to the cilium in both the GDP- and the GTP-bound form (Zhou et al, 2006; Wright et al, 2011). ARL3 binds UNC119B in a GTP-dependent fashion and is required for the ciliary localization of NPHP3 and CYS1. Upon GTPase activation, ARL3 promotes the transfer of the myristoylated cargo into the ciliary membrane (Wright et al, 2011).
Identifier: R-HSA-5624132
Species: Homo sapiens
Compartment: cilium
UNC119B promotes the translocation of myristoylated NPHP3 from the ER membrane to the cilium by an unknown mechanism. Ciliary localization depends both on myristoylation and UNC119B, as mutation of the glycine 2 acceptor site or siRNA knockdown of UNC119B drastically reduces the amount of NPHP3 or CYS1 in the cilium (Wright et al, 2011).
Identifier: R-HSA-5624130
Species: Homo sapiens
Compartment: cilium
Binding of ARL3 to UNC119B induces a conformational change that obstructs UNC119B cargo-binding and promotes the release of the myrisoylated cargo into the ciliary membrane (Wright et al, 2011; Ismail et al, 2012).
Identifier: R-HSA-5638016
Species: Homo sapiens
Compartment: cilium
ARL3 hydrolysis of GTP promotes the release of UNC119B, dissociating the complex (Wright et al, 2011; reveiwed in Schwarz et al, 2012).
Identifier: R-HSA-5638006
Species: Homo sapiens
Compartment: cilium
RP2 is an ARL3 GAP that is localized to the cilium and plays a role in trafficking proteins from the Golgi to the ciliary membrane (Veltel et al, 2008a; Hurd et al, 2011; Evans et al, 2010; Wright et al, 2011). RP2 forms a ternary complex with UNC119B and ARL3, activating the ARL3 GTPase activity and promoting the release of UNC119B (Veltel et al, 2008b; Wright et al, 2011; Kuhnel et al, 2006; reviewed in Schwarz et al, 2012; Li et al, 2012)

Complex (1 results from a total of 1)

Identifier: R-HSA-5624104
Species: Homo sapiens
Compartment: cilium

Pathway (2 results from a total of 2)

Identifier: R-HSA-5624138
Species: Homo sapiens
A number of myristoylated proteins have been shown to traffic to the cilium in a myristoyl- and UNC119B:ARL3:RP2-dependent fashion. These include the ciliary proteins Nephrocystin 3 (NPHP3) and Cystin 1 (CYS1) (Wright et al, 2011; reviewed in Schwarz et al, 2012). Myristoyl-binding by the ARL3 effector UNC119B is required in an unknown fashion for the transport of the myristoylated cargo to the cilium. At the cilium, a GTPase cycle involving the ARF-like small GTPase ARL3 and its GAP protein RP2 promote the release of the myristoylated proteins into the ciliary membrane and the recycling and ciliary exit of UNC119B (Wright et al, 2011; reviewed in Schwarz et al, 2012). ARL3 plays additional roles in the cilium coordinating the association of IFT A and IFT B complexes with the kinesin motors (Li et al, 2010; reviewed in Li et al, 2012).
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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