The ups and downs of p53: understanding protein dynamics in single cells.
Cells living in a complex environment must constantly detect, process and appropriately respond to changing signals. Therefore, all cellular information processing is dynamic in nature. As a consequence, understanding the process of signal transduction often requires detailed quantitative analysis of dynamic behaviours. Here, we focus on the oscillatory dynamics of the tumour suppressor protein p53 as a model for studying protein dynamics in single cells to better understand its regulation and function.
Harvard Medical School Systems Biology, Boston, MA 02115, USA.
Eric
E
Batchelor
Alexander
A
Loewer
Galit
G
Lahav
D000818:Animals; D064007:Ataxia Telangiectasia Mutated Proteins; D002118:Calcium / Q000378:metabolism; D018797:Cell Cycle Proteins / Q000502:physiology; D053903:DNA Breaks, Double-Stranded; D004260:DNA Repair; D004268:DNA-Binding Proteins / Q000502:physiology; D006801:Humans; D009369:Neoplasms / Q000209:etiology; D011499:Protein Processing, Post-Translational; D017346:Protein Serine-Threonine Kinases / Q000502:physiology; D015398:Signal Transduction / Q000502:physiology*; D016159:Tumor Suppressor Protein p53 / Q000502:physiology*; D025521:Tumor Suppressor Proteins / Q000502:physiology
D018797:Cell Cycle Proteins; D004268:DNA-Binding Proteins; D016159:Tumor Suppressor Protein p53; D025521:Tumor Suppressor Proteins; C576324:ATM protein, human; D064007:Ataxia Telangiectasia Mutated Proteins; D017346:Protein Serine-Threonine Kinases; D002118:Calcium