Cargo-carrying vesicles bud from the TGN

Stable Identifier
R-HSA-5623525
Type
Reaction [omitted]
Species
Homo sapiens
Compartment
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Membrane budding at the trans-Golgi network is promoted at least in part by the BAR domain of ASAP1, which is involved in sensing and inducing membrane curvature as well as providing the recognition site for small GTPases (Nie et al, 2006; Jian et al, 2009; Inoue et al, 2008; reviewed in Masuda et al, 2010). Oligomerization between ASAP1 and RAB11FIP3 may contribute to coat formation on vesicles budding from the TGN and destined for the plasma or ciliary membrane (Inoue et al, 2008; Mazelova et al, 2009; reviewed in Deretic, 2013).

Literature References
PubMed ID Title Journal Year
19153612 Ciliary targeting motif VxPx directs assembly of a trafficking module through Arf4

Mazelova, J, Astuto-Gribble, L, Inoue, H, Tam, BM, Schonteich, E, Prekeris, R, Moritz, OL, Randazzo, PA, Deretic, D

EMBO J. 2009
18685082 Arf GTPase-activating protein ASAP1 interacts with Rab11 effector FIP3 and regulates pericentrosomal localization of transferrin receptor-positive recycling endosome

Inoue, H, Ha, VL, Prekeris, R, Randazzo, PA

Mol. Biol. Cell 2008
20083215 Structural characteristics of BAR domain superfamily to sculpt the membrane

Masuda, M, Mochizuki, N

Semin. Cell Dev. Biol. 2010
16431365 A BAR domain in the N terminus of the Arf GAP ASAP1 affects membrane structure and trafficking of epidermal growth factor receptor

Nie, Z, Hirsch, DS, Luo, R, Jian, X, Stauffer, S, Cremesti, A, Andrade, J, Lebowitz, J, Marino, M, Ahvazi, B, Hinshaw, JE, Randazzo, PA

Curr. Biol. 2006
19017632 Autoinhibition of Arf GTPase-activating protein activity by the BAR domain in ASAP1

Jian, X, Brown, P, Schuck, P, Gruschus, JM, Balbo, A, Hinshaw, JE, Randazzo, PA

J. Biol. Chem. 2009
23567335 Crosstalk of Arf and Rab GTPases en route to cilia

Deretic, D

Small GTPases 2013
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