ASAP1 dimer binds membrane proteins

Stable Identifier
R-HSA-5620918
Type
Reaction [binding]
Species
Homo sapiens
Compartment
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ASAP1 is a dimeric ARF GTPase activating protein (GAP) and scaffolding protein that is recruited to the trans-Golgi network (TGN) through interactions with activated ARF4, PI(4,5)P2 and acidic phospholipids (Brown et al, 1998; Che et al, 2005; Nie et al, 2006). Once at the TGN, ASAP1 forms a tripartite complex with ARF4 and ciliary cargo, possibly by interacting with a putative C-terminal FR targeting motif present in a number of membrane proteins destined for the cilium, although this remains to be conclusively demonstrated (Corbit et al, 2005; Wang et al, 2012; reviewed in Bhogaraju et al, 2013). In addition to its role as an ARF GAP, ASAP1 also scaffolds the recruitment of a number of other proteins required for ciliary targeting, including RAB11 and the RAB11 effector FIP3 (Mazelova et al, 2009; Inoue et al, 2008; reviewed in Deretic 2013).

Literature References
PubMed ID Title Journal Year
9819391 ASAP1, a phospholipid-dependent arf GTPase-activating protein that associates with and is phosphorylated by Src

Brown, MT, Andrade, J, Radhakrishna, H, Donaldson, JG, Cooper, JA, Randazzo, PA

Mol. Cell. Biol. 1998
16136078 Vertebrate Smoothened functions at the primary cilium

Corbit, KC, Aanstad, P, Singla, V, Norman, AR, Stainier, DY, Reiter, JF

Nature 2005
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
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
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
23945166 Intraflagellar transport complex structure and cargo interactions

Bhogaraju, S, Engel, BD, Lorentzen, E

Cilia 2013
22983554 The Arf GAP ASAP1 provides a platform to regulate Arf4- and Rab11-Rab8-mediated ciliary receptor targeting

Wang, J, Morita, Y, Mazelova, J, Deretic, D

EMBO J. 2012
23567335 Crosstalk of Arf and Rab GTPases en route to cilia

Deretic, D

Small GTPases 2013
16038802 Regulation of ASAP1 by phospholipids is dependent on the interface between the PH and Arf GAP domains

Che, MM, Boja, ES, Yoon, HY, Gruschus, J, Jaffe, H, Stauffer, S, Schuck, P, Fales, HM, Randazzo, PA

Cell. Signal. 2005
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