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Lynxl and the β2V287L Mutation Affect the Stoichiometry of the α4β2 Nicotinic Acetylcholine Receptor


Nichols, Weston A. (2014) Lynxl and the β2V287L Mutation Affect the Stoichiometry of the α4β2 Nicotinic Acetylcholine Receptor. Dissertation (Ph.D.), California Institute of Technology. doi:10.7907/2S9B-R910.


GPI-anchored neurotoxin-like receptor binding proteins, such as lynx modulators, are topologically positioned to exert pharmacological effects by binding to the extracellular portion of nAChRs. These actions are generally thought to proceed when both lynx and the nAChRs are on the plasma membrane. Here, we demonstrate that lynx1 also exerts effects on α4β2 nAChRs within the endoplasmic reticulum. Lynx affects assembly of nascent α4 and β2 subunits, and alters the stoichiometry of the population that reaches the plasma membrane. Additionally, these data suggest that lynx1 alters nAChR stoichiometry primarily through this intracellular interaction, rather than via effects on plasma membrane nAChRs. To our knowledge, these data represent the first test of the hypothesis that a lynx family member, or indeed any GPI-anchored protein, could act within the cell to alter assembly of multi-subunit protein.

Item Type:Thesis (Dissertation (Ph.D.))
Subject Keywords:lynx1, nicotinic acetylcholine receptor, endoplasmic reticulum, GPI-anchor
Degree Grantor:California Institute of Technology
Division:Biology and Biological Engineering
Major Option:Neurobiology
Thesis Availability:Public (worldwide access)
Research Advisor(s):
  • Lester, Henry A.
Thesis Committee:
  • Deshaies, Raymond Joseph (chair)
  • Dougherty, Dennis A.
  • Prober, David A.
  • Lester, Henry A.
Defense Date:1 May 2014
Non-Caltech Author Email:weston.a.nichols (AT)
Record Number:CaltechTHESIS:05292014-190146869
Persistent URL:
Default Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:8430
Deposited By: Weston Nichols
Deposited On:03 Jun 2014 18:59
Last Modified:04 Oct 2019 00:05

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