Words similar to gα
Example sentences for: gα
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The A326S mutation of α i1 and A366S mutation of α s (cognate to the α i2 A327S used in this study) were shown to cause greatly decreased affinity for GDP [ 9 10 ] . Defective binding of GDP leads to more Gα in the empty state (no bound guanine-nucleotide), and this form of Gα is rapidly denatured in vitro , as shown for α s A366S and α i1 A326S [ 9 10 ] . Moreover, α s A366S was demonstrated to undergo rapid degradation (t 1/2 < 1 h) in stably transfected cells [ 9 ] . The same mutation in α t has also been shown to greatly decrease guanine-nucleotide binding [ 5 22 ] . Additional amino acids in the critical β6-α5 loop are important for maintaining Gα integrity [ 7 ] .
These results are also consistent with the possibility that the primary defect in sα i2 is a reduced ability to interact with βγ; Gα containing mutations in known sites of contact with βγ fail to localize to PM, but over-expression of βγ can rescue their PM localization [ 28 29 ] . However, the crystal structures [ 30 31 ] show that the C-terminal β6-α5 loop/α5 helix region does not directly contact βγ.
Based on this unique localization of sα i2 , a prominent role in membrane trafficking has been proposed for this subunit [ 3 ] . However, no report to date has supported a functional role for sα i2 in vesicular transport, although a variety of functional assays have implicated other Gα, including α s and α i3 , in vesicle trafficking pathways [ 1 2 ] .
Although the α5 helix (Figure 1) does not directly contact the bound guanine-nucleotide [ 19 20 21 ] , it is clearly important for Gα structure and to maintain the proper orientation of the β6-α5 loop.
Second, the extreme C-termini of Gα are critical sites for interaction with GPCRs [ 32 ] , and the novel C-terminal sequence found in sα i2 would be predicted to disrupt productive interactions with GPCRs.
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