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GTP is required to stabilize and display transamidation activity of transglutaminase 2.

Abstract：

:Transglutaminase 2 (TGase 2) is a bifunctional enzyme that catalyzes calcium-dependent transamidation and GTP binding/hydrolysis. The transamidation activity is proposed to be associated with several neurodegenerative disorders such as Alzheimer's and Hungtinton's disease. However, the regulation mechanism by which TGase 2 causes neurodegeneration is unknown. In this study, we show that two activities of TGase 2 have a differential stability; transamidation activity is less stable than GTP hydrolytic activity, and that GTP was required to stabilize and to display transamidation activity. Moreover, GTP binding-defective mutant of TGase 2 did not show any transamidation activity in transfection experiments. These results indicate that GTP binding is crucial for transamidation activity of TGase 2, suggesting that protein cross-linking by TGase 2 might be associated with G-protein coupled receptor signaling system. Thus, our data could contribute to understand the regulation of TGase 2 activity and TGase 2-associated pathogenesis.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Jeon JH,Cho SY,Kim CW,Shin DM,Kweon JC,Choi KH,Park SC,Kim IG

doi

10.1016/S0006-291X(02)00582-X

subject

Has Abstract

pub_date

2002-06-21 00:00:00

pages

818-22

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(02)00582-X

journal_volume

294

pub_type

杂志文章

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