Regulation of the activities of the mammalian transglutaminase family of enzymes

Cornelius Klöck; Chaitan Khosla

doi:10.1002/pro.2162

journal article Nov 09, 2012

Regulation of the activities of the mammalian transglutaminase family of enzymes

Cornelius Klöck Chaitan Khosla

Protein Science Vol. 21 No. 12 pp. 1781-1791 · Wiley

View at Publisher Save 10.1002/pro.2162

Abstract

AbstractMammalian transglutaminases catalyze post‐translational modifications of glutamine residues on proteins and peptides through transamidation or deamidation reactions. Their catalytic mechanism resembles that of cysteine proteases. In virtually every case, their enzymatic activity is modulated by elaborate strategies including controlled gene expression, allostery, covalent modification, and proteolysis. In this review, we focus on our current knowledge of post‐translational regulation of transglutaminase activity by physiological as well as synthetic allosteric agents. Our discussion will primarily focus on transglutaminase 2, but will also compare and contrast its regulation with Factor XIIIa as well as transglutaminases 1 and 3. Potential structure–function relationships of known mutations in human transglutaminases are analyzed.

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References

87

[1]

10.1038/nrm1014

[2]

10.1152/physrev.00044.2008

[3]

Mehta K (2005)

[4]

10.1152/physrev.00016.2010

[5]

10.1016/b978-0-12-394305-7.00001-x

[6]

10.1073/pnas.042454899

[7]

10.1371/journal.pbio.0050327

[8]

10.1016/0014-5793(88)80928-1

[9]

10.1111/j.1742-4658.2009.07420.x

[10]

10.1016/0167-4838(87)90222-6

[11]

10.1074/jbc.m600146200

[12]

10.1007/s00726-009-0442-5

[13]

10.1371/journal.pone.0001861

[14]

10.1016/s0021-9258(18)96373-8

[15]

Boothe R "A reversible, calcium‐dependent, copper‐catalyzed inactivation of guinea pig liver transglutaminase" J Biol Chem (1969) 10.1016/s0021-9258(18)94444-3

[16]

10.1074/jbc.m111.287490

[17]

10.1074/jbc.m109.097162

[18]

10.1016/s0968-0004(02)02182-5

[19]

10.1038/nrm1150

[20]

10.1152/ajplung.00082.2012

[21]

10.2741/1863

[22]

10.1021/bi00428a032

[23]

10.1126/science.7911253

[24]

10.1074/jbc.m111.337089

[25]

10.1074/jbc.m111.294819

[26]

10.1186/1471-2407-12-277

[27]

10.1002/jcb.23278

[28]

10.1021/jm060839a

[29]

10.1016/s0968-0896(01)00101-8

[30]

10.1016/s1074-5521(03)00045-0

[31]

10.1016/j.pharmthera.2007.05.003

[32]

10.1021/jo8004843

[33]

10.1021/bi701422h

[34]

10.1007/s00432-009-0645-x

[35]

10.1021/bi061787u

[36]

10.1016/j.bmcl.2010.12.037

[37]

10.1016/j.bmcl.2005.02.005

[38]

10.1177/1087057110366035

[39]

10.1016/s0021-9258(18)41717-6

[40]

10.1016/0167-4781(95)00219-7

[41]

10.1096/fj.06-7598com

[42]

10.1073/pnas.0604844103

[43]

10.1096/fj.01-0689com

[44]

10.1002/humu.9511

[45]

10.1111/j.1742-4658.2011.08345.x

[46]

10.1530/jme-11-0064

[47]

10.1074/jbc.m010846200

[48]

10.1128/mcb.21.1.148-155.2001

[49]

The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling

Konstantin Arnold, Lorenza Bordoli, Jürgen Kopp et al.

Bioinformatics 10.1093/bioinformatics/bti770

[50]

10.1002/humu.20952

Showing 50 of 87 references

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Citations

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References

Details

Published: Nov 09, 2012
Vol/Issue: 21(12)
Pages: 1781-1791
License: View

Authors

Stanford University

Cite This Article

Cornelius Klöck, Chaitan Khosla (2012). Regulation of the activities of the mammalian transglutaminase family of enzymes. Protein Science, 21(12), 1781-1791. https://doi.org/10.1002/pro.2162

Regulation of the activities of the mammalian transglutaminase family of enzymes

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