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Human Serotonin Transporter Coding Variation Establishes Conformational Bias with Functional Consequences.

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Rare autism spectrum disorder (ASD) variants in the serotonin transporter (SERT) cause hyperfunction by altering its conformation. This leads to altered serotonin clearance and ASD-associated traits, highlighting SERT

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Genetics

Background:

  • The serotonin transporter (SERT) regulates neurotransmitter levels, crucial for brain function.
  • Rare variants in SERT are linked to autism spectrum disorder (ASD).
  • Previous studies identified SERT variants with increased transport activity in ASD families.

Purpose of the Study:

  • To elucidate the physical basis of hyperfunction for the common ASD-associated SERT variant, Ala56.
  • To investigate mutation-induced conformational changes in SERT.
  • To determine if these conformational changes impact transporter function and regulation.

Main Methods:

  • Fluorescence resonance energy transfer (FRET) assays to study N- and C-termini interactions.
  • Methanethiosulfonate sensitivity assays.
  • N-terminal tryptic digestion experiments.
  • In vitro and in vivo assessments.

Main Results:

  • SERT Ala56 variant exhibits altered conformation, favoring an open-outward state.
  • This conformational change is associated with altered 5-HT binding affinity (Km).
  • Similar conformational changes were observed with another ASD-associated variant, Asn605.

Conclusions:

  • Heritable SERT variants can induce biased transporter conformations.
  • These biased conformations impact SERT function and regulation.
  • Altered SERT conformation is a potential mechanism underlying ASD-associated traits.