Plasticity of PDZ domains in ligand recognition and signaling.

作者: Ylva Ivarsson

DOI: 10.1016/J.FEBSLET.2012.04.015

关键词: PDZ domainPhospholipid BindingCell signalingPeptidePhosphorylationAllosteric regulationBiologyFunction (biology)Scaffold proteinCell biology

摘要: The PDZ domain is a protein–protein interacting module that plays an important role in the organization of signaling complexes. recognition short intrinsically disordered C-terminal peptide motifs archetypical function, but functional repertoire this versatile also includes internal sequences, dimerization and phospholipid binding. function can be tuned by various means such as allosteric effects, changes physiological buffer conditions phosphorylation domains and/or ligands, which poses dynamic regulators cell signaling. This review focused on plasticity interactions.

参考文章(141)
Tracy T. Cao, Heather W. Deacon, David Reczek, Anthony Bretscher, Mark von Zastrow, A kinase-regulated PDZ-domain interaction controls endocytic sorting of the β2-adrenergic receptor Nature. ,vol. 401, pp. 286- 290 ,(1999) , 10.1038/45816
Beom Sik Kang, David R. Cooper, Yancho Devedjiev, Urszula Derewenda, Zygmunt S. Derewenda, Molecular roots of degenerate specificity in syntenin's PDZ2 domain: reassessment of the PDZ recognition paradigm. Structure. ,vol. 11, pp. 845- 853 ,(2003) , 10.1016/S0969-2126(03)00125-4
Timothy B.C. London, Ho-Jin Lee, Youming Shao, Jie Zheng, Interaction between the internal motif KTXXXI of Idax and mDvl PDZ domain. Biochemical and Biophysical Research Communications. ,vol. 322, pp. 326- 332 ,(2004) , 10.1016/J.BBRC.2004.07.113
Xin Shao, Lijun Zhu, Yubin Wang, Yuting Lu, Wenhai Wang, Jia Zhu, Ying Shen, Jun Xia, Jianhong Luo, Threonine 82 at the PDZ domain of PICK1 is critical for AMPA receptor interaction and localization. Neurochemistry International. ,vol. 56, pp. 962- 970 ,(2010) , 10.1016/J.NEUINT.2010.04.006
A. Ernst, S. L. Sazinsky, S. Hui, B. Currell, M. Dharsee, S. Seshagiri, G. D. Bader, S. S. Sidhu, Rapid evolution of functional complexity in a domain family. Science Signaling. ,vol. 2, ,(2009) , 10.1126/SCISIGNAL.2000416
Stefano Mostarda, David Gfeller, Francesco Rao, Beyond the Binding Site: The Role of the β2 – β3 Loop and Extra-Domain Structures in PDZ Domains PLOS Computational Biology. ,vol. 8, ,(2012) , 10.1371/JOURNAL.PCBI.1002429
Young Jun Im, Jun Hyuck Lee, Seong Ho Park, Soo Jeong Park, Seong-Hwan Rho, Gil Bu Kang, Eunjoon Kim, Soo Hyun Eom, Crystal structure of the Shank PDZ-ligand complex reveals a class I PDZ interaction and a novel PDZ-PDZ dimerization Journal of Biological Chemistry. ,vol. 278, pp. 48099- 48104 ,(2003) , 10.1074/JBC.M306919200
Kimberly A. Reynolds, Richard N. McLaughlin, Rama Ranganathan, Hot spots for allosteric regulation on protein surfaces. Cell. ,vol. 147, pp. 1564- 1575 ,(2011) , 10.1016/J.CELL.2011.10.049
Darren J. Park, Christopher J. Wallick, Kendra D. Martyn, Alan F. Lau, Chengshi Jin, Bonnie J. Warn-Cramer, Akt Phosphorylates Connexin43 on Ser373, a “Mode-1” Binding Site for 14-3-3 Cell Communication & Adhesion. ,vol. 14, pp. 211- 226 ,(2007) , 10.1080/15419060701755958
Sarah M. Garrard, Christopher T. Capaldo, Lin Gao, Michael K. Rosen, Ian G. Macara, Diana R. Tomchick, Structure of Cdc42 in a complex with the GTPase-binding domain of the cell polarity protein, Par6 The EMBO Journal. ,vol. 22, pp. 1125- 1133 ,(2003) , 10.1093/EMBOJ/CDG110