Natalia Jura, PhD

Professor, Cardiovascular Research Institute
Research Interests: 
Mechanisms of Receptor Tyrosine Kinase signaling

Research Summary:
Receptor tyrosine kinases, kinase regulatory mechanisms, membrane proteins, feedback regulation of cell signaling Summary: We study basic mechanisms of cellular signaling by Receptor Tyrosine Kinases with a goal to understand how cells receive and process growth signals provided by the neighboring cells and the extracellular milieu. Receptor Tyrosine Kinases are single pass transmembrane receptors that catalyze tyrosine phosphorylation upon activation of their intracellular kinase domains. These receptors are principal regulators of growth and survival signals in cells and therefore frequently become deregulated in human diseases. We are interested in understanding how the kinase activity of these receptors is regulated by ligand binding and how the receptors associate with their regulatory components during the activation process. By combining biochemistry and cell biology we are studying these processes in the reconstituted membrane systems in vitro and in the plasma membrane of the living cells. We also use crystallography to gain an atomic resolution insight into Receptor Tyrosine Kinase regulation that will help us design new approaches for therapeutic intervention.

Address: 
555 & 535 Mission Bay Blvd Sou, Rm 452W
UCSF Box 3122
San Francisco, CA 94158
United States
Phone: 
+1 415 514-1133
Faculty Type: 
Core CVRI Faculty
Publications: 

Structures of the PI3Kα/KRas complex on lipid bilayers reveal the molecular mechanism of PI3Kα activation.(link is external)

bioRxiv : the preprint server for biology

Torosyan H, Paul MD, Maker A, Meyer BG, Jura N, Verba KA

Mapping kinase domain resistance mechanisms for the MET receptor tyrosine kinase via deep mutational scanning.(link is external)

eLife

Estevam GO, Linossi E, Rao J, Macdonald CB, Ravikumar A, Chrispens KM, Capra JA, Coyote-Maestas W, Pimentel H, Collisson EA, Jura N, Fraser JS

Mapping kinase domain resistance mechanisms for the MET receptor tyrosine kinase via deep mutational scanning.(link is external)

bioRxiv : the preprint server for biology

Estevam GO, Linossi EM, Rao J, Macdonald CB, Ravikumar A, Chrispens KM, Capra JA, Coyote-Maestas W, Pimentel H, Collisson EA, Jura N, Fraser JS

G3BP isoforms differentially affect stress granule assembly and gene expression during cellular stress.(link is external)

Molecular biology of the cell

Liboy-Lugo JM, Espinoza CA, Sheu-Gruttadauria J, Park JE, Xu A, Jowhar Z, Gao AL, Carmona-Negrón JA, Wittmann T, Jura N, Floor SN

Conserved regulatory motifs in the juxtamembrane domain and kinase N-lobe revealed through deep mutational scanning of the MET receptor tyrosine kinase domain.(link is external)

eLife

Estevam GO, Linossi EM, Macdonald CB, Espinoza CA, Michaud JM, Coyote-Maestas W, Collisson EA, Jura N, Fraser JS

Conserved regulatory motifs in the juxtamembrane domain and kinase N-lobe revealed through deep mutational scanning of the MET receptor tyrosine kinase domain.(link is external)

bioRxiv : the preprint server for biology

Estevam GO, Linossi EM, Macdonald CB, Espinoza CA, Michaud JM, Coyote-Maestas W, Collisson EA, Jura N, Fraser JS

Protein-protein interactions with G3BPs drive stress granule condensation and gene expression changes under cellular stress.(link is external)

bioRxiv : the preprint server for biology

Liboy-Lugo JM, Espinoza CA, Sheu-Gruttadauria J, Park JE, Xu A, Jowhar Z, Gao AL, Carmona-Negrón JA, Wittmann T, Jura N, Floor SN

Hedgehog target genes regulate lipid metabolism to drive basal cell carcinoma and medulloblastoma.(link is external)

Research square

Daggubati V, Vykunta A, Choudhury A, Qadeer Z, Mirchia K, Saulnier O, Zakimi N, Hines K, Paul M, Wang L, Jura N, Xu L, Reiter J, Taylor M, Weiss W, Raleigh D

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