Post-Translational Modifications


A Major Focus for the Future of Proteomics

Gerald W. Hart and Lauren E. Ball

December 2013 Ruan et al article in Molecular & Cellular Proteomics

With 20,000 to 30,000 human genes and only 100,000 expressed proteins, the dynamic complexity of living systems is achieved, in part, through an enormous repertoire of chemical modifications of amino acids that occur during and after protein translation. There are over 400 known post-translational modifications (PTMs), and technical advances in methodology and instrumentation are permitting the discovery of new modifications, enabling the development of a global view of the role of modifications in responding to and regulating biological processes, and revealing the magnitude of complexity that is imparted to protein regulation by combinations of modifications. PTMs encode information regarding the status of the cell and synergistically modify polypeptide functions in a manner that is highly responsive to both cellular metabolism and external cues. In fact, it is the myriad molecular species created by multiple PTMs of a polypeptide that represent the biologically functional end point of gene expression. As analytical methods continue to improve, it will likely become a major focus of biomedical and other types of molecular research to elucidate the functions of the many different isoforms of polypeptides, which must eventually be understood first at the individual site level on polypeptides and ultimately by defining the structure/functions of individual molecular species with multiple PTMs.

December 2013 Ruan et al article in Molecular & Cellular Proteomics

This special issue of Molecular and Cellular Proteomics grew out of the bi-annual Special Symposium “Post Translational Modifications: Detection and Physiological Roles” held at Lake Tahoe in October of 2012, which was supported by the American Society for Biochemistry and Molecular Biology (ASBMB) and Molecular and Cellular Proteomics. Papers in this issue illustrate ongoing work in the field of PTMs that builds upon the advances in proteomics made during the past decades.

Fairman Studios

To visually capture the complex intricacies of the molecular biology involved in post-translational modifications, certified medical illustrator Jennifer Fairman designed several of the figures as well as its cover art. Fairman is the Founder and Principal of Fairman Studios and is an Assistant Professor in the Department of Art as Applied to Medicine (AAM, medart) at the Johns Hopkins University School of Medicine where she previously received her Master of Arts in Medical and Biological Illustration.

December 2013 Ruan et al article in Molecular & Cellular Proteomics

AAM is a leader in the field of visual communication for science and health care. Built on a strong foundation of scientific knowledge, artistic technique, and clear visual communication, AAM has maintained the highest standards while embracing new medical, scientific, and communication technologies. The faculty produces illustrations, animations, and graphic design for the medical, research and publishing communities. Concurrently, AAM educates future medical illustrators through a two-year, accredited, Master of Arts program in Medical and Biological Illustration. Recognized internationally for over 100 years, its graduates continue the Hopkins Tradition of Excellence into the 21st century.

December 2013 Ruan et al article in Molecular & Cellular Proteomics

Articles in this issue

Post-translational Modifications: A Major Focus for the Future of Proteomics

Gerald W. Hart and Lauren E. Ball

First Published on November 25, 2013, doi:10.1074/mcp.E113.036491

Status of Large-scale Analysis of Post-translational Modifications by Mass Spectrometry

Jesper V. Olsen and Matthias Mann

First Published on November 1, 2013, doi:10.1074/mcp.O113.034181

The Coming of Age of Phosphoproteomics—from Large Data Sets to Inference of Protein Functions

Philippe P. Roux and Pierre Thibault

First Published on September 13, 2013, doi:10.1074/mcp.R113.032862

Large-scale Top-down Proteomics of the Human Proteome: Membrane Proteins, Mitochondria, and Senescence

Adam D. Catherman, Kenneth R. Durbin, Dorothy R. Ahlf, Bryan P. Early, Ryan T. Fellers, John C. Tran, Paul M. Thomas, and Neil L. Kelleher

First Published on September 10, 2013, doi:10.1074/mcp.M113.030114

N- and O-Glycosylation in the Murine Synaptosome

Jonathan C. Trinidad, Ralf Schoepfer, Alma L. Burlingame, and Katalin F. Medzihradszky

First Published on July 1, 2013, doi:10.1074/mcp.M113.030007

Regulation of Protein Degradation by O-GlcNAcylation: Crosstalk with Ubiquitination

Hai-Bin Ruan, Yongzhan Nie, and Xiaoyong Yang

First Published on July 3, 2013, doi:10.1074/mcp.R113.029751

Spatiotemporal Dynamics of Phosphorylation in Lipid Second Messenger Signaling

Corina E. Antal and Alexandra C. Newton

First Published on June 20, 2013, doi:10.1074/mcp.R113.029819

Identification of Lysine Succinylation Substrates and the Succinylation Regulatory Enzyme CobB in Escherichia coli

Gozde Colak, Zhongyu Xie, Anita Y. Zhu, Lunzhi Dai, Zhike Lu, Yi Zhang, Xuelian Wan, Yue Chen, Yoon H. Cha, Hening Lin, Yingming Zhao, and Minjia Tan

First Published on October 31, 2013, doi:10.1074/mcp.M113.031567

Using the Ubiquitin-modified Proteome to Monitor Protein Homeostasis Function 

Andrea C. Carrano and Eric J. Bennett

First Published on May 23, 2013, doi:10.1074/mcp.R113.029744

Proteolytic Post-translational Modification of Proteins: Proteomic Tools and Methodology

Lindsay D. Rogers and Christopher M. Overall

First Published on July 25, 2013, doi:10.1074/mcp.M113.031310

Alpha-synuclein Post-translational Modifications as Potential Biomarkers for Parkinson Disease and Other Synucleinopathies

Adrien W. Schmid, Bruno Fauvet, Marc Moniatte, and Hilal A. Lashuel

First Published on August 21, 2013, doi:10.1074/mcp.R113.032730

Stable Isotope Metabolic Labeling-based Quantitative Phosphoproteomic Analysis of Arabidopsis Mutants Reveals Ethylene-regulated Time-dependent Phosphoproteins and Putative Substrates of Constitutive Triple Response 1 Kinase

Zhu Yang, Guangyu Guo, Manyu Zhang, Claire Y. Liu, Qin Hu, Henry Lam, Han Cheng, Yu Xue, Jiayang Li, and Ning Li

First Published on September 16, 2013, doi:10.1074/mcp.M113.031633