2002
DOI: 10.1074/jbc.c200481200
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Characterization of a Fast Cycling ADP-ribosylation Factor 6 Mutant

Abstract: Studies of GTPase function often employ expression of dominant negative or constitutively active mutants. Dominant negative mutants cannot bind GTP and thus cannot be activated. Constitutively active mutants cannot hydrolyze GTP and therefore accumulate a large pool of GTP-bound GTPase. These mutations block the normal cycle of GTP binding, hydrolysis, and release. Therefore, although the GTPase-deficient mutants are in the active conformation, they do not fully imitate all the actions of the GTPase. This is p… Show more

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Cited by 52 publications
(62 citation statements)
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References 35 publications
(47 reference statements)
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“…Thus, they do not sequester effectors and are less prone to artifacts that may affect the interpretation of results. A rapid cycling Arf6 mutant, T157A, has been previously characterized (19). For this study, we generated a corresponding Arf5 mutant, Arf5(T161A), which also exhibits enhanced binding to the effector protein GGA3, similar to its Arf6 counterpart (Fig.…”
Section: Brag2mentioning
confidence: 99%
See 1 more Smart Citation
“…Thus, they do not sequester effectors and are less prone to artifacts that may affect the interpretation of results. A rapid cycling Arf6 mutant, T157A, has been previously characterized (19). For this study, we generated a corresponding Arf5 mutant, Arf5(T161A), which also exhibits enhanced binding to the effector protein GGA3, similar to its Arf6 counterpart (Fig.…”
Section: Brag2mentioning
confidence: 99%
“…For this study, we generated a corresponding Arf5 mutant, Arf5(T161A), which also exhibits enhanced binding to the effector protein GGA3, similar to its Arf6 counterpart (Fig. 3E) (19).…”
Section: Brag2mentioning
confidence: 99%
“…The ARF6 mutants used included dominant-negative ARF6 T27N, which is defective in GTP binding, and fast cycling T157A, which is spontaneously more active than the wild-type protein (Santy, 2002). The latter mutant binds and releases GTP more quickly and induces phenotypes characteristic of ARF6 activation without disrupting the normal functions of the protein (Donaldson, 2003).…”
Section: Arf6 Promotes Spine Formationmentioning
confidence: 99%
“…7C, lane 2). The same was true for the activated form of Arf1 (Arf1 T161A), which was generated based on a previously reported fast-cycling Arf6 mutant (28). However, interestingly, when the activated Arf1 and Arf6 mutants were co-expressed in NIH3T3 cells, colony formation in soft agar was enhanced (Fig.…”
Section: Resultsmentioning
confidence: 73%
“…The QuikChange TM Site-Directed Mutagenesis kit (Stratagene) was used to generate point mutants of Cat-1 that are defective in binding Cool-1 (D294K/E295R) (24), paxillin (K663E/K758E) (25), or are defective as an Arf-GAP (R39A) (26). Likewise, dominant active forms of Arf1 (Q71L, T161A) (27,28) and Arf6 (D125N) (29), as well as dominant negative Arf6 (T27N) (30), were also generated.…”
Section: Methodsmentioning
confidence: 99%