Exocyst complex component 2 is a protein that in humans is encoded by the EXOC2gene.[1][2][3]
The protein encoded by this gene is a component of the exocyst complex, a multiple protein complex essential for targeting exocytic vesicles to specific docking sites on the plasma membrane. Though best characterized in yeast, the component proteins and the functions of the exocyst complex have been demonstrated to be highly conserved in higher eukaryotes. At least eight components of the exocyst complex, including this protein, are found to interact with the actin cytoskeletal remodeling and vesicle transport machinery. This interaction has been shown to mediate filopodia formation in fibroblasts.[3]
References
↑Murthy M, Garza D, Scheller RH, Schwarz TL (Feb 2003). "Mutations in the exocyst component Sec5 disrupt neuronal membrane traffic, but neurotransmitter release persists". Neuron. 37 (3): 433–47. doi:10.1016/S0896-6273(03)00031-X. PMID12575951.
↑Sjolinder M, Uhlmann J, Ponstingl H (Dec 2002). "DelGEF, a homologue of the Ran guanine nucleotide exchange factor RanGEF, binds to the exocyst component Sec5 and modulates secretion". FEBS Lett. 532 (1–2): 211–5. doi:10.1016/S0014-5793(02)03677-3. PMID12459492.
Hsu SC, Hazuka CD, Roth R, et al. (1998). "Subunit composition, protein interactions, and structures of the mammalian brain sec6/8 complex and septin filaments". Neuron. 20 (6): 1111–22. doi:10.1016/S0896-6273(00)80493-6. PMID9655500.
Mott HR, Nietlispach D, Hopkins LJ, et al. (2003). "Structure of the GTPase-binding domain of Sec5 and elucidation of its Ral binding site". J. Biol. Chem. 278 (19): 17053–9. doi:10.1074/jbc.M300155200. PMID12624092.
Moskalenko S, Tong C, Rosse C, et al. (2004). "Ral GTPases regulate exocyst assembly through dual subunit interactions". J. Biol. Chem. 278 (51): 51743–8. doi:10.1074/jbc.M308702200. PMID14525976.
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