Michael Ferns

image of Michael Ferns



Physiology and Membrane Biology
Anesthesiology & Pain Medicine

Offices and Labs

(530) 754 4973

Profile Introduction

Synapse formation in mammalian nervous system.


1988 PhD Neurobiology Univ of Western Australia
1983 B.Sc. (Hons) Physiology Univ of Otago

Research Interests

Cellular and molecular basis of cholinergic synapse formation in mammalian nervous system

My interest is in understanding the cellular and molecular basis of synapse formation in the mammalian nervous system. Synapse formation is critical for the formation, maintenance and plasticity of the nervous system and perturbations in synaptic structure and function have been implicated in a range of neurological disorders. My research focuses on cholinergic synapses that play critical roles in the functioning of both the peripheral and central nervous systems. Our main aims are (1) to define the extracellular synaptogenic factors that regulate the formation and maintenance of neuromuscular and neuronal autonomic synapses in the PNS; (2) to define the intracellular mechanisms that regulate the trafficking and localization of nicotinic acetylcholine receptors at these synapses; and (3) to establish how defects in synapse formation or receptor localization contribute to neurological diseases such as myasthenia gravis and congenital myasthenic syndromes. 

Department and Center Affiliations

Anesthesiology & Pain Medicine
Physiology and Membrane Biology


Society for Neuroscience

CBS Grad Group Affiliations

Molecular, Cellular, and Integrative Physiology
Biochemistry, Molecular, Cellular and Developmental Biology

Specialties / Focus

Molecular, Cellular, and Integrative Physiology
  • Neurophysiology
  • Molecular Physiology
  • Cellular Physiology
Biochemistry, Molecular, Cellular and Developmental Biology
  • Cell Biology
  • Developmental Biology
  • Neurobiology


Ferns lab / Tupper Hall, Rm 4215
  • Jolene Chang, MD/PhD student; John Rudell, PhD student


MCP 210A Advanced Physiology (Fall)
HPH 400 Human Physiology (Fall)


1/31/2013 3:29:06 PM
  • Gingras, J., Rassadi, S., Cooper, E., & Ferns, M. 2002 Agrin plays an organizing role in the formation of sympathetic synapses. J. Cell Biol. 158(6):1109-1118.
  • Gingras, J., Spicer, J., Altares, M., Zhu, Q., Kuchel, G.A. and Ferns, M. (2005) Agrin becomes concentrated at neuroeffector junctions in developing rodent urinary bladder. Cell & Tissue Research, 320: 115-125.
  • Gingras, J., Rassadi, S., Cooper, E., and Ferns, M. (2007) Synaptic transmission is impaired at neuronal autonomic synapses in agrin null mice. Dev. Neurobiol. 67(5): 521-534.
  • Lee, Y., Rudell, J., Yechikhov, S., Taylor, R., Swope, S., and Ferns, M. (2008) Rapsyn carboxyl terminal domains mediate muscle specific kinase-induced phosphorylation of the muscle acetylcholine receptor. Neuroscience, 153: 997-1007.
  • Borges LS, Yechikhov S, Lee YI, Rudell JB, Friese MB, Burden SJ, Ferns MJ (2008) Identification of a motif in the acetylcholine receptor beta subunit whose phosphorylation regulates rapsyn association and postsynaptic receptor localization. J Neurosci. 28:11468-11476.

    * Selected by Faculty of 1000 as a “Must-Read” article

  • Lee Y, Rudell J, and Ferns M. (2009) Rapsyn interacts with the muscle acetylcholine receptor via alpha-helical domains in the alpha, beta and epsilon subunit intracellular loops. Neuroscience 163:222-232.
  • Maselli, RA., Fernandez, JM., Arredondo, J., Navarro, C., Ngo, M., Beeson, D., Cagney, O., Williams, DC., Wollmann, RL., and Yarov-Yarovoy, V., and Ferns, M. (2012) LG2 agrin mutation causing severe congenital myasthenic syndrome mimics functional characteristics of non-neural (z-) agrin. Human Genetics 131(7): 1123-35.
  • Rudell, JB., and Ferns, MJ. (2013) Regulation of muscle acetylcholine receptor turnover by β subunit tyrosine phosphorylation. Dev. Neurobiol. 73(5):399-410.

    * Selected by Faculty of 1000 Prime

  • Chang Rudell, J., Borges, LS., Rudell, JB., Beck, KA., and Ferns, MJ. (2014) Determinants in the beta and delta subunit cytoplasmic loop regulate Golgi trafficking and surface expression of the muscle acetylcholine receptor. J. Biol. Chem.  289(1):203-214.