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HyDegronomics

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Cracking the Code for Protein Quality Control Mechanisms Recognizing Exposed Hyd...

Cracking the Code for Protein Quality Control Mechanisms Recognizing Exposed Hydrophobicity in Protein Substrates Proteostasis is a highly regulated process by which cells maintain a healthy proteome. Loss of proteostasis is a common feature of aging and disease. To preserve proteostasis, the cell has developed protein quality control (PQC) p... ver más

31/01/2026

BIU

2M€

Presupuesto del proyecto: 2M€

Líder del proyecto

BAR ILAN UNIVERSITY No se ha especificado una descripción o un objeto social para esta compañía.

TRL 4-5

Ver 2 Participantes

Financiación concedida El organismo H2020 notifico la concesión del proyecto el día 2020-11-03

ERC-2020-STG: ERC STARTING GRANTS

I+D

Cerrada hace 5 años

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2 Participantes

BIU

1.80M€ | Lider

PLASTICOS SOPLADOS TECNICOS...

587.39K€ | Participante

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Duración del proyecto: 62 meses Fecha Inicio: 2020-11-03
Fecha Fin: 2026-01-31

Líder del proyecto

BAR ILAN UNIVERSITY No se ha especificado una descripción o un objeto social para esta compañía.

TRL 4-5

Presupuesto del proyecto 2M€

Descripción del proyecto Proteostasis is a highly regulated process by which cells maintain a healthy proteome. Loss of proteostasis is a common feature of aging and disease. To preserve proteostasis, the cell has developed protein quality control (PQC) pathways that monitor a proteins’s fate from synthesis to degradation. Exposed hydrophobic residues in aberrant or mislocalized protein substrates is a key feature recognized by distinct PQC mechanisms. If not handled properly, exposed hydrophobicity can result in protein aggregation and subsequent reduced cell fitness. To prevent accumulation of toxic aggregates, cells are equipped both with chaperones and proteolytic pathways. Within the degradation systems, E3 ligases are the major determinants of specificity, which is achieved through their selective recognition of specific short peptide motifs, or degrons, in substrate proteins. Despite the growing list of PQC players and substrates, it has yet to be determined what are the client range, selectivity and specificity of each of the PQC mechanisms. The objective of this proposal is to systematically investigate the exposed hydrophobicity code and to advance the state-of-the-art of the PQC field. Here, we utilize the GPS-peptidome method that we recently developed together with genetics, biochemistry, cell biology and proteomic approaches to: (1) map distinct classes of hydrophobic degrons to elucidate the specificity of substrate selection; (2) identify novel E3 ligases playing a role in PQC pathways, explore redundancies among them and identify endogenous substrates proteome- wide; (3) investigate the physiological significance of PQC mechanisms. This work will provide a comprehensive view of PQC pathways that recognize hydrophobicity. This is critical to further our understanding on how aberrant features in proteins are recognized and can provide valuable information for the development of new therapeutic intervention strategies that target abnormal proteins implicated in disease.

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