Reactome | RGGT binds the RAB-binding subunit

RGGT binds the RAB-binding subunit

Stable Identifier

R-HSA-8870465

Type

Reaction [binding]

Species

Homo sapiens

Compartment

cytosol

ReviewStatus

5/5

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The catalytic dimer of RGGTA and B interacts with RAB-escorting proteins 1 or 2 (CHM and CHML, also known as REP-1 and REP-2) to form a functional trimeric RAB geranylgeranyl transferase complex that is capable of binding and geranylgeranylating newly synthesized RAB proteins (Baron and Seabra, 2008; reviewed in Leung et al, 2006; Gutkowska and Swiezewska, 2012). There are two models for the formation of a functional enzyme:substrate complex. In the classical model, unprenylated RAB first binds to REP and is subsequently presented to the catalytic subunits of the GGTase. Incorporation of geranylgeranyl pyrophosphate (GGPP) strengthens the interaction between enzyme and substrate (Andres et al, 1993; Thoma et al, 2001a). In the alternate route, which is depicted in this pathway, RGGTA and RGGTB first bind to REP in a GGPP-dependent manner in the absence of the RAB substrate. Unprenylated RABs then bind to the fully formed GGTase for geranylgeranylation (Thoma et al, 2001b; Baron and Seabra, 2008).

Literature References

PubMed ID	Title	Journal	Year
22694141	Structure, regulation and cellular functions of Rab geranylgeranyl transferase and its cellular partner Rab Escort Protein Swiezewska, E, Gutkowska, M	Mol. Membr. Biol.	2012
8513495	cDNA cloning of component A of Rab geranylgeranyl transferase and demonstration of its role as a Rab escort protein Cremers, FP, Seabra, MC, Armstrong, SA, Andres, DA, Smeland, TE, Goldstein, JL, Brown, MS	Cell	1993
16401880	Thematic review series: lipid posttranslational modifications. geranylgeranylation of Rab GTPases Seabra, MC, Leung, KF, Baron, R	J. Lipid Res.	2006
18532927	Rab geranylgeranylation occurs preferentially via the pre-formed REP-RGGT complex and is regulated by geranylgeranyl pyrophosphate Seabra, MC, Baron, RA	Biochem. J.	2008
11675392	Phosphoisoprenoids modulate association of Rab geranylgeranyltransferase with REP-1 Iakovenko, A, Goody, RS, Thomä, NH, Alexandrov, K	J. Biol. Chem.	2001
11141079	Allosteric regulation of substrate binding and product release in geranylgeranyltransferase type II Alexandrov, K, Iakovenko, A, Waldmann, H, Thomä, NH, Kalinin, A, Goody, RS	Biochemistry	2001