TY - JOUR
T1 - Capturing dynamic protein interactions
T2 - A method based on heat denaturation reveals how proteins interact in different cells
AU - Li, Xiao Han
AU - Chavali, Pavithra L.
AU - Babu, M. Madan
N1 - Copyright © 2018 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works
PY - 2018/3/9
Y1 - 2018/3/9
N2 - Protein-protein interactions form the molecular basis for organismal development and function (1, 2). In cells, protein interactions are dynamic and subject to spatiotemporal regulations that are specific to the cell type and cell cycle phase. Mutations that abolish or rewire protein-protein interaction networks (the interactome) are often detrimental and manifest in developmental anomalies and diseases (3, 4). Recent advances in quantitative proteomics offer snapshots of cell type–specific proteomes, but scientific understanding of how protein-protein interactions vary between physiological and disease conditions is limited. On page 1170 of this issue, Tan et al. report a technique for inferring dynamics of protein interactions by characterizing protein thermal stability upon heat denaturation (5).
AB - Protein-protein interactions form the molecular basis for organismal development and function (1, 2). In cells, protein interactions are dynamic and subject to spatiotemporal regulations that are specific to the cell type and cell cycle phase. Mutations that abolish or rewire protein-protein interaction networks (the interactome) are often detrimental and manifest in developmental anomalies and diseases (3, 4). Recent advances in quantitative proteomics offer snapshots of cell type–specific proteomes, but scientific understanding of how protein-protein interactions vary between physiological and disease conditions is limited. On page 1170 of this issue, Tan et al. report a technique for inferring dynamics of protein interactions by characterizing protein thermal stability upon heat denaturation (5).
UR - http://www.scopus.com/inward/record.url?scp=85043300953&partnerID=8YFLogxK
U2 - 10.1126/science.aat0576
DO - 10.1126/science.aat0576
M3 - Comment/debate
C2 - 29590031
AN - SCOPUS:85043300953
SN - 0036-8075
VL - 359
SP - 1105
EP - 1106
JO - Science
JF - Science
IS - 6380
ER -