A 'molecular switchboard'--covalent modifications to proteins and their impact on transcription.
Proteins undergo a remarkable variety of posttranslational modifications, with more than 200 distinct modifications identified to date. Increasing evidence suggests that many proteins bear multiple, distinct modifications, and the ability of one modification to antagonize or synergize the deposition of another can have significant biological consequences. Here, we illustrate the importance of posttranslational modifications within the context of transcriptional regulation, and we offer a perspective on the emerging role of combinatorial networks of modifications. Finally, we discuss the potential for chemical approaches to transform our understanding of the field.
Khidekel
Nelly
N
Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.
Hsieh-Wilson
Linda C
LC
D000595:Amino Acid Sequence; D000818:Animals; D017362:Cyclic AMP Response Element-Binding Protein / Q000737:chemistry / Q000502:physiology; D006657:Histones / Q000737:chemistry; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000737:chemistry / Q000378:metabolism* / Q000502:physiology; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D012319:RNA Polymerase II / Q000737:chemistry; D014158:Transcription, Genetic; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry / Q000502:physiology
D017362:Cyclic AMP Response Element-Binding Protein; D006657:Histones; D009687:Nuclear Proteins; D016159:Tumor Suppressor Protein p53; D012319:RNA Polymerase II