TY - JOUR
T1 - Function, evolution, and structure of J-domain proteins
AU - Kampinga, Harm H.
AU - Andreasson, Claes
AU - Barducci, Alessandro
AU - Cheetham, Michael E.
AU - Cyr, Douglas
AU - Emanuelsson, Cecilia
AU - Genevaux, Pierre
AU - Gestwicki, Jason E.
AU - Goloubinoff, Pierre
AU - Huerta-Cepas, Jaime
AU - Kirstein, Janine
AU - Liberek, Krzysztof
AU - Mayer, Matthias P.
AU - Nagata, Kazuhiro
AU - Nillegoda, Nadinath B.
AU - Pulido, Pablo
AU - Ramos, Carlos
AU - De los Rios, Paolo
AU - Rospert, Sabine
AU - Rosenzweig, Rina
AU - Sahi, Chandan
AU - Taipale, Mikko
AU - Tomiczek, Bratlomiej
AU - Ushioda, Ryo
AU - Young, Jason C.
AU - Zimmermann, Richard
AU - Zylicz, Alicja
AU - Zylicz, Maciej
AU - Craig, Elizabeth A.
AU - Marszalek, Jaroslaw
PY - 2019/1
Y1 - 2019/1
N2 - Hsp70 chaperone systems are very versatile machines present in nearly all living organisms and in nearly all intracellular compartments. They function in many fundamental processes through their facilitation of protein (re)folding, trafficking, remodeling, disaggregation, and degradation. Hsp70 machines are regulated by co-chaperones. J-domain containing proteins (JDPs) are the largest family of Hsp70 co-chaperones and play a determining role functionally specifying and directing Hsp70 functions. Many features of JDPs are not understood; however, a number of JDP experts gathered at a recent CSSI-sponsored workshop in Gdansk (Poland) to discuss various aspects of J-domain protein function, evolution, and structure. In this report, we present the main findings and the consensus reached to help direct future developments in the field of Hsp70 research.
AB - Hsp70 chaperone systems are very versatile machines present in nearly all living organisms and in nearly all intracellular compartments. They function in many fundamental processes through their facilitation of protein (re)folding, trafficking, remodeling, disaggregation, and degradation. Hsp70 machines are regulated by co-chaperones. J-domain containing proteins (JDPs) are the largest family of Hsp70 co-chaperones and play a determining role functionally specifying and directing Hsp70 functions. Many features of JDPs are not understood; however, a number of JDP experts gathered at a recent CSSI-sponsored workshop in Gdansk (Poland) to discuss various aspects of J-domain protein function, evolution, and structure. In this report, we present the main findings and the consensus reached to help direct future developments in the field of Hsp70 research.
KW - Heat shock protein 70 (Hsp70)
KW - J-domain proteins (JDPs)
KW - 8-stranded -sandwich domain (SBD)
KW - HEAT-SHOCK PROTEINS
KW - ENDOPLASMIC-RETICULUM
KW - HSP70 CHAPERONE
KW - MOLECULAR CHAPERONES
KW - DNAJ
KW - SUBSTRATE
KW - RELEASE
KW - HSC70
KW - AGGREGATION
KW - SUPPRESSION
UR - https://www.scopus.com/pages/publications/85057304619
U2 - 10.1007/s12192-018-0948-4
DO - 10.1007/s12192-018-0948-4
M3 - Review article
SN - 1355-8145
VL - 24
SP - 7
EP - 15
JO - Cell stress & chaperones
JF - Cell stress & chaperones
IS - 1
ER -