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Cited by 18Protein Kinase Regulation and GTPase SignalingNeuroscience and Neuropharmacology ResearchCalpain Protease Function and Regulation

Brain Region and Isoform-Specific Phosphorylation Alters Kalirin SH2 Domain Interaction Sites and Calpain Sensitivity

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Miller, Megan B., Yan, Yan, Machida, Kazuya, Kiraly, Drew D., Levy, Aaron D., Wu, Yi I., Lam, TuKiet T., Abbott, Thomas +3 more·2017·ACS Chemical Neuroscience
DOI 10.1021/acschemneuro.7b00076PMC PMC5517348
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Abstract

Kalirin7 (Kal7), a postsynaptic Rho GDP/GTP exchange factor (RhoGEF), plays a crucial role in long-term potentiation and in the effects of cocaine on behavior and spine morphology. The KALRN gene has been linked to schizophrenia and other disorders of synaptic function. Mass spectrometry was used to quantify phosphorylation at 26 sites in Kal7 from individual adult rat nucleus accumbens and prefrontal cortex before and after exposure to acute or chronic cocaine. Region- and isoform-specific phosphorylation was observed along with region-specific effects of cocaine on Kal7 phosphorylation. Evaluation of the functional significance of multisite phosphorylation in a complex protein like Kalirin is difficult. With the identification of five tyrosine phosphorylation (pY) sites, a panel of 71 SH2 domains was screened, identifying subsets that interacted with multiple pY sites in Kal7. In addition to this type of reversible interaction, endoproteolytic cleavage by calpain plays an essential role in long-term potentiation. Calpain cleaved Kal7 at two sites, separating the N-terminal domain, which affects spine length, and the PDZ binding motif from the GEF domain. Mutations preventing phosphorylation did not affect calpain sensitivity or GEF activity; phosphomimetic mutations at specific sites altered protein stability, increased calpain sensitivity, and reduced GEF activity.

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  • CaMKII phosphorylates Kalirin at T75, and this phosphorylation is sufficient to enhance synaptic transmission.

    “CaMKII phosphorylates Kalirin at T75 (Ref. 315, but see Ref. 317), and this phosphorylation is sufficient to enhance synaptic transmission.”

    From Synaptic memory and CaMKII (2023) · cites this paper as [317]

    In Results and Discussion (‘Kalirin phosphorylation is brain region specific’; page unavailable), the paper says its in vitro studies found CaMKII phosphorylation at T79, not the T75 site named in the claim. The cited passage also does not show that phosphorylation at T75 is sufficient to enhance synaptic transmission. (LLM, conf=0.83)

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  • RhoGEFs kalirin-7, Trio, and Tiam are expressed in spines and phosphorylated by CaMKII.

    “The RhoGEFs that have received the most attention are kalirin-7, Trio, and Tiam, which are all expressed in spines and phosphorylated by CaMKII (314–317).”

    From Synaptic memory and CaMKII (2023) · cites this paper as [317]

    The Results and Discussion section (page unavailable) states that Kal7 is concentrated at the postsynaptic density and that in vitro studies show CaMKII phosphorylates Kal7 at T79. The paper does not establish that Trio or Tiam are expressed in spines or phosphorylated by CaMKII, so it supports the claim only for kalirin-7. (LLM, conf=0.90)

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Cited by

Sorted by citations

Authors
Miller, M. B., Yan, Y., Machida, K., Kiraly, D. D., Levy, A. D., Wu, Y. I., Lam, T. T., Abbott, T., Koleske, A. J., Eipper, B. A., & Mains, R. E.
Affiliations
  • UConn Health (US)
  • Yale University (US)
  • Icahn School of Medicine at Mount Sinai (US)
Corresponding author
  • Machida, Kazuya
  • Mains, Richard E.
ORCID
Venue
ACS Chemical Neuroscience
Publisher
American Chemical Society (ACS)
Published
2017-04-25
Volume
8
Issue
7
Pages
1554-1569
ISSN
1948-7193 (ISSN-L)
DOI
10.1021/acschemneuro.7b00076
PMC
PMC5517348
OpenAlex
W2606845713
Cited by
18
References
4
Citations by year
2025: 1 · 2024: 2 · 2023: 1 · 2022: 2 · 2021: 4 · 2020: 3 · 2019: 4 · 2018: 1
FWCI
0.89
Type
journal article
Language
en
Open access
Locations
  • ACS Chemical Neuroscience (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
National Institute of Diabetes and Digestive and Kidney Diseases (DK-32948)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Calpain Protease Function and Regulation
Keywords
KALRN, multisite phosphorylation, tyrosine phosphorylation, calpain cleavage, RhoGEF, nucleus accumbens, prefrontal cortex, cocaine exposure, long-term potentiation, synaptic plasticity, PDZ-binding motif, phosphomimetic mutations, protein stability, schizophrenia
MeSH terms
Animals, Binding Sites, Calpain, Cocaine, Humans, Male, Nucleus Accumbens, Phosphorylation, Mass Spectrometry, Tyrosine, Rats, Sprague-Dawley, Prefrontal Cortex, Dopamine Uptake Inhibitors, src Homology Domains, Protein Isoforms, Guanine Nucleotide Exchange Factors, rac1 GTP-Binding Protein, PDZ Domains, HEK293 Cells

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