MEMPART

Membrane partitioning of homologous proteins

 Coordinatore STICHTING KATHOLIEKE UNIVERSITEIT 

Spiacenti, non ci sono informazioni su questo coordinatore. Contattare Fabio per maggiori infomrazioni, grazie.

 Nazionalità Coordinatore Netherlands [NL]
 Totale costo 1˙500˙000 €
 EC contributo 1˙500˙000 €
 Programma FP7-IDEAS-ERC
Specific programme: "Ideas" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
 Code Call ERC-2013-StG
 Funding Scheme ERC-SG
 Anno di inizio 2013
 Periodo (anno-mese-giorno) 2013-12-01   -   2018-11-30

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    STICHTING KATHOLIEKE UNIVERSITEIT

 Organization address address: GEERT GROOTEPLEIN NOORD 9
city: NIJMEGEN
postcode: 6525 EZ

contact info
Titolo: Dr.
Nome: Geert
Cognome: Van Den Bogaart
Email: send email
Telefono: 31243613662
Fax: 31243540339

NL (NIJMEGEN) hostInstitution 1˙500˙000.00
2    STICHTING KATHOLIEKE UNIVERSITEIT

 Organization address address: GEERT GROOTEPLEIN NOORD 9
city: NIJMEGEN
postcode: 6525 EZ

contact info
Titolo: Mr.
Nome: Wim
Cognome: Van Oijen
Email: send email
Telefono: 31243618937

NL (NIJMEGEN) hostInstitution 1˙500˙000.00

Mappa


 Word cloud

Esplora la "nuvola delle parole (Word Cloud) per avere un'idea di massima del progetto.

closely    protein    organization    partitioning    homologous    membrane    clustering    proteins    partition    snare    distinct    membranes    mechanisms    lipid    domains    cellular    elucidate    selective    model   

 Obiettivo del progetto (Objective)

'My goal is to elucidate how structurally closely-related proteins are selectively partitioned in distinct membrane domains that allow localization, clustering and segregation of specific cellular activities. Although many of the mechanisms that govern membrane organization are increasingly well understood, such as lipid ‘rafts’ or protein-anchoring to the cortical cytoskeleton, these mechanisms are not sufficiently specific to account for the partitioning of closely homologous proteins in separate membrane domains. I believe that the observed highly selective membrane partitioning can only be explained by the combined action of protein-protein and protein-lipid interactions and thermodynamic properties of the membrane (length, charge, degree of hydrophobicity). I aim to gain a full understanding of how homologous proteins partition in distinct functional membrane domains by studying SNARE proteins as a model system. Different SNAREs partition in different domains with different degrees of overlap in the plasma membrane where they catalyze the final membrane fusion steps of various exocytotic pathways. I will employ quantitative super-resolution microscopy to study the effects of selective (biochemical and genetic) perturbations on SNARE partitioning in both precisely controllable artificial membranes and in PC12 cells. This will allow me to elucidate the mechanisms, contributions and interplay of individual membrane clustering mechanisms in SNARE domain organization. I then plan to demonstrate that the mechanisms of SNARE partitioning explain the membrane organization of other (homologous) proteins as well. My ultimate ambitious goal is to generate a complete model of how proteins are organized in biological membranes. I anticipate that my findings will uncover new and general mechanisms of membrane organization and, since membranes are involved in almost all cellular processes, my work may have impact on virtually all areas of the health and life sciences.'

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