Jose Ramón Bayascas Ramírez

Jose Ramón Bayascas Ramírez

 

Jose Ramón Bayascas Ramírez

Academic Staff

Phone:
+34 935 813 762

Email:
joseramon.bayascas@uab.cat

Adress:

Department of Biochemistry and Molecular Biology
Institut de Neurociències
Faculty  of Medicine (room M2-115.1)
Universitat Autònoma de Barcelona (UAB)
Bellaterra Campus 08193-Cerdanyola del Vallés

Area

Thesis number in address


Jose Ramon Bayascas was born and educated in Barcelona, were he graduated in Biological Sciences from the University of Barcelona in 1992 and received a Ph.D. in Biological Sciences in 1998 under the supervision of Professor Emili Saló, University of Barcelona. He then carried out postdoctoral research for nine years, first with Professor Joan Comella at the University of Lleida from 1998 to 2002, and then with Professor Dario Alessi at the University of Dundee, Scotland, from 2002 to 2007, were he became proficient in the analysis of cell signaling in metabolism, cancer and neurobiology. In 2007 he joined the Departament de Bioquímica i Biologia Molecular of the Universitat Autònoma de Barcelona, were he has been the group leader of a new research team ever since, first as a Ramon y Cajal Fellow and from October 2014 as a Serra Húnter Associate Professor. His current research aims to define the neurodevelopmental functions of the PDK1 signaling network and its consequences to neurodegenerative and mental disease.

Dr. Bayascas is a Principal Investigator at the Signaling and New Therapeutic Targets (SINDATER) research group and leads his own laboratory:
 
 

Group members:
Sònia Pascual

Former members:
Tinatin Zurashvili
Patricia Ortega
Juuli Lamberg
Esther Cabañas
Natalia Gorska
Laura Kempainnen                   
Shaobin Yang
LLuís Cordón Barris
Xiangyu Zhou
Rebeca Ponce
Carlota Niemeyer
Anna Fosch
Anna de Bolòs
 

 
 
RESEARCH INTEREST
 
Understand the importance that the dysfunction of the mechanisms of signal transduction might play in brain pathology. They focussed on the PI 3-kinase/Akt signaling pathway, which controls essential roles during neuronal development and is deregulated in different mental disorders. They generated brain-specific conditional knock-in mice expressing two distinct rationally designed, crystal structure-based, point mutant forms of the PDK1 kinase, a master hub on this signaling pathway. In the PDK1 K465E mice, activation of Akt is selectively impaired, whereas in the PDK1 L155E mice, activation of most of the effectors of this signaling axis including S6K, RSK, SGK, and PKC, but not Akt, is abolished.
 

CURRENT WORK
 
The neurodevelopmental consequences of these genetic signaling lesions have already been extensively characterized, and two research lines have emerged:
 
1) To investigate whether the PDK1 K465E mice is protected from Alzheimer Disease. In the PDK1 K465E knock-in mice, reduced activation of Akt caused subtle morphogenetic defects that did not lead however to adverse behavioral outputs. We learned that the hypomorphic reduction of the Akt axis protected these mice from a number of insults disrupting homeostasis, which might singularly be also protected from neurodegeneration.
 
2) To define the contribution of the PDK1 substrates different from Akt to mental disease. In the PDK1 L155E mice, the normal and exclusive activation of Akt among the different PDK1 substrates caused profound defects in the patterning of the central nervous system, leading to severe mental disorders reminiscent of human schizophrenia.

 

  • Zhou X, Cordon-Barris L, Zurashvili T, Bayascas JR. (2014) Fine-tuning the intensity of the PKB/Akt signal enables diverse physiological responses. Cell Cycle. 13:3164-8.
  • Erazo T, Moreno A, Ruiz-Babot G, Rodríguez-Asiain A, Morrice NA, Espadamala J, Bayascas JR, Gómez N, Lizcano JM. (2013) Canonical and kinase activity-independent mechanisms for extracellular signal-regulated kinase 5 (ERK5) nuclear translocation require dissociation of Hsp90 from the ERK5-Cdc37 complex. Mol Cell Biol. 33:1671-86.
  • Zurashvili T, Cordón-Barris L, Ruiz-Babot G, Zhou X, Lizcano JM, Gómez N, Giménez-Llort L, Bayascas JR. (2013) Interaction of PDK1 with phosphoinositides is essential for neuronal differentiation but dispensable for neuronal survival. Mol Cell Biol. 33:1027-40.
  • Rodríguez-Asiain A, Ruiz-Babot G, Romero W, Cubí R, Erazo T, Biondi RM, Bayascas JR, Aguilera J, Gómez N, Gil C, Claro E, Lizcano JM. (2011) Brain specific kinase-1 BRSK1/SAD-B associates with lipid rafts: modulation of kinase activity by lipid environment. Biochim Biophys Acta. 1811:1124-35.
  • Bayascas JR. (2010) PDK1: the major transducer of PI 3-kinase actions. Curr Top Microbiol Immunol. 346:9-29.
  • ·     Sanchez Canedo C, Demeulder B, Ginion A, Bayascas JR, Balligand JL, Alessi DR, Vanoverschelde JL, Beauloye C, Hue L, Bertrand L. (2010) Activation of the cardiac mTOR/p70(S6K) pathway by leucine requires PDK1 and correlates with PRAS40 phosphorylation. Am J Physiol Endocrinol Metab. 298:761-9.
  •  Waugh C, Sinclair L, Finlay D, Bayascas JR, Cantrell D. (2009) Phosphoinositide (3,4,5)-triphosphate binding to phosphoinositide-dependent kinase 1 regulates a protein kinase B/Akt signaling threshold that dictates T-cell migration, not proliferation. Mol Cell Biol. 29:5952-62.
  • Bayascas JR. (2008) Dissecting the role of the 3-phosphoinositide-dependent protein kinase-1 (PDK1) signalling pathways. Cell Cycle. 7:2978-82.
  • Bayascas JR, Wullschleger S, Sakamoto K, García-Martínez JM, Clacher C, Komander D, van Aalten DM, Boini KM, Lang F, Lipina C, Logie L, Sutherland C, Chudek JA, van Diepen JA, Voshol PJ, Lucocq JM, Alessi DR. (2008) Mutation of the PDK1 PH domain inhibits protein kinase B/Akt, leading to small size and insulin resistance. Mol Cell Biol. 28:3258-72.
  • Alessi DR, Sakamoto K, Bayascas JR. (2006) LKB1-dependent signaling pathways. Annu Rev Biochem. 75:137-63.
  • Bayascas JR, Sakamoto K, Armit L, Arthur JS, Alessi DR. (2006) Evaluation of approaches to generation of tissue-specific knock-in mice. J Biol Chem. 281:28772-81.
  • Bayascas JR, Leslie NR, Parsons R, Fleming S, Alessi DR. (2005) Hypomorphic mutation of PDK1 suppresses tumorigenesis in PTEN(+/-) mice. Curr Biol. 15:1839-46.
  • Bayascas JR, Alessi DR. (2005) Regulation of Akt/PKB Ser473 phosphorylation. Mol Cell. 18:143-5.
  • Cordón-Barris L, Pascual-Guiral S, Yang S, Giménez-Llort L, Lope-Piedrafita S, Niemeyer C, Claro E, Lizcano JM, Bayascas JR. Mutation of the 3-phosphoinositide-dependent protein kinase-1 (PDK1) substrate-docking site in the developing brain causes microcephaly with abnormal brain morphogenesis independently of Akt, leading to impaired cognition and disruptive behaviors. Mol Cell Biol. 2016 36: 2967-82.
     

 

See all JR. Bayascas publications at PubMed.

Institut de Neurociències
Tel: 93 581 3861 / Fax: +34 93 581 3327

Facultat de Medicina. Edifici M-1
Avinguda de Can Domènech - Campus de la UAB · 08193
Bellaterra (Cerdanyola del Vallès) · Barcelona