An Rtn4/Nogo-A-interacting micropeptide modulates synaptic plasticity with age.

Autor: Kragness S; Department of Cell and Molecular Biology, Tulane University, New Orleans, LA, United States of America., Clark Z; Department of Cell and Molecular Biology, Tulane University, New Orleans, LA, United States of America., Mullin A; Department of Cell and Molecular Biology, Tulane University, New Orleans, LA, United States of America.; Tulane University Transgenic Core Facility, New Orleans, LA, United States of America., Guidry J; Department of Biochemistry and Molecular Biology, LSU School of Medicine and Health Sciences Center, New Orleans, LA, United States of America.; The Proteomics Core Facility, LSUHSC, New Orleans, LA, United States of America., Earls LR; Department of Cell and Molecular Biology, Tulane University, New Orleans, LA, United States of America.
Jazyk: angličtina
Zdroj: PloS one [PLoS One] 2022 Jun 30; Vol. 17 (6), pp. e0269404. Date of Electronic Publication: 2022 Jun 30 (Print Publication: 2022).
DOI: 10.1371/journal.pone.0269404
Abstrakt: Micropeptides, encoded from small open reading frames of 300 nucleotides or less, are hidden throughout mammalian genomes, though few functional studies of micropeptides in the brain are published. Here, we describe a micropeptide known as the Plasticity-Associated Neural Transcript Short (Pants), located in the 22q11.2 region of the human genome, the microdeletion of which conveys a high risk for schizophrenia. Our data show that Pants is upregulated in early adulthood in the mossy fiber circuit of the hippocampus, where it exerts a powerful negative effect on long-term potentiation (LTP). Further, we find that Pants is secreted from neurons, where it associates with synapses but is rapidly degraded with stimulation. Pants dynamically interacts with Rtn4/Nogo-A, a well-studied regulator of adult plasticity. Pants interaction with Nogo-A augments its influence over postsynaptic AMPA receptor clustering, thus gating plasticity at adult synapses. This work shows that neural micropeptides can act as architectural modules that increase the functional diversity of the known proteome.
Competing Interests: The authors have declared that no competing interests exist.
Databáze: MEDLINE
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