Johannes W. Hell

Johannes Hell

Position Title
Professor

Unit
Department of Pharmacology, School of Medicine

2419D Tupper Hall
Bio

Research Interests

Dr. Hell’s laboratory works on the molecular and cellular mechanisms of neurotransmission at synapses in the brain.

We study the molecular architecture of the postsynaptic site of glutamatergic synapses in the mammalian brain. We use biochemical, cell biological and electrophysiological methods to investigate how various structural proteins anchor postsynaptic glutamate receptors. We  investigate how  postsynaptic signaling by calcium influx and by protein kinase A (PKA) and other kinases and phosphatases defines postsynaptic glutamate receptor trafficking and accumulation under physiological conditions as occurring during learning. We also study mechanisms underlying Alzheimer’s disease and PTSD.

Grad Group Affiliations

  • Biochemistry, Molecular, Cellular and Developmental Biology
  • Neuroscience
  • Pharmacology and Toxicology (PTX)

Specialties / Focus

  • Biochemistry
  • Cell Biology
  • Neurobiology
  • Signal Transduction

Courses

  • PHA 205 Problem Solving in Pharmacological Sciences, Fall, Winter, Spring

Professional Societies

  • Society for Neuroscience

Degrees

  • 1991 PhD Biochemistry University of Munich

Publications

MA Davare, V Avdonin, DD Hall, EM Peden, A Burette, RJ Weinberg, MC Horne, T Hoshi, and J W. Hell (2001): A b2 adrenergic receptor signaling complex assembled with the Ca2+ channel Cav1.2.  Science 293, 98-101.

K-U Bayer, P De Koninck, AS Leonard, JW Hell, and H Schulman (2001): Interaction with the NMDA receptor locks CaMKII in an active conformation.  Nature 411, 801-804.

Y Lu, ML Allen, AR Halt, M Weisenhaus, RF Dallapiazza, DD Hall, YM Usachev,  GS McKnight, and JW Hell (2007): Age-dependent  requirement of AKAP150-anchored PKA and GluR2-lacking AMPA receptors in LTP.  EMBO J 26, 4879-4890.

Z Akyol Ataman, L Gakhar, BR Sorensen, JW Hell, and MA Shea (2007): The NMDA Receptor NR1 C1 Region Bound to Calmodulin: Structural Insights into Functional Differences Between Homologous Domains.  Structure 15, 1603-1617.

MA Joiner, M-F Lise, EY Yuen, AYF Kam, M Zhang, DD Hall, Z Malik, H Qian, Y Chen, JD Ulrich, AC Burette, RJ  Weinberg, P-Y Law, A El-Husseini, Z Yan, and JW Hell (2010): Assembly of a b2 adrenergic receptor – GluR1 signaling complex for localized cAMP signaling. EMBO J 29, 482-495.

JA Bartos, H Li, MA Beazely, JD Ulrich, Y Chen, JF MacDonald, and JW Hell (2010): Postsynaptic clustering and activation of Pyk2 by PSD-95.  J Neurosci 30, 449-463.

AR Halt*, RF Dallapiazza*, Y Zhou, IS Stein, H Qian, S Juntti, S Wojcik, N Brose, AJ Silva, and JW Hell (2012): CaMKII binding to GluN2B is critical during memory consolidation. EMBO J 31, 1203-1216 (*the two first-authors made equal contributions).

AM Hamilton, WC Oh, H Vega-Ramirez, IS Stein, JW Hell, GN Patrick, and K Zito (2012): Activity-dependent growth of new dendritic spines is regulated by the proteasome.  Neuron  74, 1023-1030.

DD Hall*, S Dai*, P-Y Tseng*, ZA Malik, M Nguyen, L Matt, K Schnizler, A Shephard, DP Mohapatra, F Tsuruta, RE Dolmetsch, CJ Christel, A Lee, A Burette, RJ Weinberg, and JW Hell (2013): Competition between a-actinin and Ca2+-calmodulin controls surface retention of the L-type Ca2+ channel Cav1.2. Neuron 78, 483-497 (*co-first authors).

Y Zhang*, L Matt*, T Patriarchi*, ZA Malik, D Chowdhury, DK Park, A Renieri, JB Ames**, and JW Hell** (2014): Capping of the N-terminus of PSD-95 by Calmodulin Triggers its Postsynaptic Release. EMBO J 33,1341-1353  (*co-first authors; **co-corresponding authors).

JW Hell (2014) CaMKII: claiming center stage in postsynaptic function and organization. Neuron 81, 249-265.

K He, M Huertas, SZ Hong, XX Tie, JW Hell, H Shouval, A Kirkwood (2015). Distinct Eligibility Traces for LTP and LTD in Cortical Synapses. Neuron 88, 528-538.

T Patriarchi, H Qian, V Di Biase, ZA Malik, D Chowdhury, JL Price, EA Hammes, OR Buonarati, RE Westenbroek, WA Catterall, F Hofmann, YK Xiang, GG Murphy, C-Y Chen, MF Navedo, and JW Hell (2015): Phosphorylation of Cav1.2 on S1928 uncouples the L-type Ca2+ channel from the b2 adrenergic receptor.  EMBO J 36, 1330-1345.

H Qian, T Patriarchi, JL Price, L Matt, B Lee, M Nieves-Cintrón, OR Buonarati, D Chowdhury, E Nanou, MA Nystoriak, WA Catterall, M Poomvanicha, F Hofmann, MF Navedo*, and JWHell* (2017): Phosphorylation of Ser1928 mediates the enhanced L-type Cav1.2 channel activity by the b2-adrenergic receptor in neurons. Science Signaling 10, eaaf9659 (*Co-senior authors).

MA Nystoriak, M Nieves-Cintrón, T Patriarchi, OR Buonarati, M Paz Prada, S Morotti, E Grandi, J Dos Santos Fernandes, K Forbush, F Hofmann, KC Sasse, JD Scott, SM Ward, JW Hell, and MF Navedo (2017): Ser1928 phosphorylation by PKA stimulates the L-type Ca2+ channel and vasoconstriction during acute hyperglycemia and diabetes. Science Signaling 10, eaaf9647.

DJ Goodell, V Zaegel, SJ Coultrap, JW Hell, and K-U Bayer (2017): DAPK1 mediates LTD by making CaMKII/GluN2B binding LTP-specific. Cell Rep 19, 2231-2243.

D Chowdhury*, D Turner*, T Patriarchi, AC Hergarden, D Anderson, Y Zhang, J Sun, C-Y Chen, JB Ames**, and JW Hell** (2017): Ca2+/Calmodulin Binding to PSD-95 Mediates Homeostatic Synaptic Scaling Down. EMBO J, in press (*Co-first authors; **Co-senior authors).

 

Tags