J-domain proteins: From molecular mechanisms to diseases

Marszalek, Jaroslaw; De Los Rios, Paolo; Cyr, Douglas; Mayer, Matthias P.; Adupa, Vasista; Andréasson, Claes; Blatch, Gregory L.; Braun, Janice E.A.; Brodsky, Jeffrey L.; Bukau, Bernd; Chapple, J. Paul; Conz, Charlotte; Dementin, Sébastien; Genevaux, Pierre; Genest, Olivier; Goloubinoff, Pierre; Gestwicki, Jason; Hammond, Colin M.; Hines, Justin K.; Ishikawa, Koji; Joachimiak, Lukasz A.; Kirstein, Janine; Liberek, Krzysztof; Mokranjac, Dejana; Nillegoda, Nadinath; Ramos, Carlos H.I.; Rebeaud, Mathieu; Ron, David; Rospert, Sabine; Sahi, Chandan; Shalgi, Reut; Tomiczek, Bartlomiej; Ushioda, Ryo; Ustyantseva, Elizaveta; Ye, Yihong; Zylicz, Maciej; Kampinga, Harm H.

doi:10.1016/j.cstres.2023.12.002

Cited by 7 publications

(2 citation statements)

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“…JDPs are grouped into three classes—A, B, and C—depending on their domain structure ( Marszalek et al, 2024 ). Class A and B JDPs share a similar architecture, while JDPs possessing any other architecture are placed in Class C. Class A and B JDPs have an N-terminal, 4-helix J-domain typically followed by a glycine-rich region and two β-sandwich domains, followed by a C-terminal dimerization domain.…”

Section: Introductionmentioning

confidence: 99%

“…Class A and B JDPs share a similar architecture, while JDPs possessing any other architecture are placed in Class C. Class A and B JDPs have an N-terminal, 4-helix J-domain typically followed by a glycine-rich region and two β-sandwich domains, followed by a C-terminal dimerization domain. By definition, members of Class A have a zinc-binding domain protruding from the N-terminal β-sandwich, while members of Class B do not (see Figure 1A ) ( Marszalek et al, 2024 ). Four Class A/B JDPs are present in the cytosol of Saccharomyces cerevisiae ( Sahi and Craig, 2007 ); three belong to Class A: Ydj1, Apj1, and Xdj1.…”

Section: Introductionmentioning

confidence: 99%

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Unique characteristics of the J-domain proximal regions of Hsp70 cochaperone Apj1 in prion propagation/elimination and its overlap with Sis1 function

Ganser,

McNish,

Schwanitz

et al. 2024

Front. Mol. Biosci.

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J-domain proteins (JDPs) are obligate cochaperones of Hsp70s. The Class A JDP Apj1 of the yeast cytosol has an unusually complex region between the N-terminal J-domain and the substrate binding region—often called the Grich or GF region in Class A and B JDPs because of its typical abundance of glycine. The N-terminal 161-residue Apj1 fragment is known to be sufficient for Apj1 function in prion curing, driven by the overexpression of Hsp104. Further analyzing the N-terminal segment of Apj1, we found that a 90-residue fragment that includes the 70-residue J-domain and the adjacent 12-residue glutamine/alanine (Q/A) segment is sufficient for curing. Furthermore, the 121-residue fragment that includes the Grich region was sufficient to not only sustain the growth of cells lacking the essential Class B JDP Sis1 but also enabled the maintenance of several prions normally dependent on Sis1 for propagation. A J-domain from another cytosolic JDP could substitute for the Sis1-related functions but not for Apj1 in prion curing. Together, these results separate the functions of JDPs in prion biology and underscore the diverse functionality of multi-domain cytosolic JDPs in yeast.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%