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A\u03b2 stimulates the \u03b2\n                  <jats:sub>2<\/jats:sub>\n                  adrenergic receptor (\u03b2\n                  <jats:sub>2<\/jats:sub>\n                  AR), which forms a unique signaling complex with the L-type Ca\n                  <jats:sup>2+<\/jats:sup>\n                  channel (LTCC) Ca\n                  <jats:sub>V<\/jats:sub>\n                  1.2. LTCCs have been implicated in the etiology of dementia and AD. We show that A\u03b2 acutely potentiates Ca\n                  <jats:sub>V<\/jats:sub>\n                  1.2 via the \u03b2\n                  <jats:sub>2<\/jats:sub>\n                  AR, which triggers postsynaptic recruitment of Ca\n                  <jats:sup>2+<\/jats:sup>\n                  permeable (CP) AMPARs in hippocampal cultures and impairs LTP in hippocampal slices within minutes. The long-term consequence is a loss of postsynaptic structure of glutamatergic synapses and neurotoxicity. Disrupting this signaling cascade with highly specific tools prevented all of these effects, unifying a number of currently divergent findings on A\u03b2 synaptotoxicity including dysregulation of AMPARs and synaptic plasticity.\n                <\/jats:p>\n                <jats:sec>\n                  <jats:title>TEASER<\/jats:title>\n                  <jats:p>\n                    Amyloid \u03b2 peptide is the primary pathological agent in Alzheimer\u2019s disease. It affects the nanoscale structure and function of glutamatergic synapses. The molecular mechanisms are largely unknown except for identification of several binding proteins including the \u03b2\n                    <jats:sub>2<\/jats:sub>\n                    adrenergic receptor. We show that this binding potently (EC\n                    <jats:sub>50<\/jats:sub>\n                    &lt;100 nM) augments Ca\n                    <jats:sup>2+<\/jats:sup>\n                    influx through the L-type Ca channel Ca\n                    <jats:sub>V<\/jats:sub>\n                    1.2. This effect leads to improper recruitment of Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -permeable glutamate receptors to postsynaptic sites (EC\n                    <jats:sub>50<\/jats:sub>\n                    &lt;100 nM), synaptic dysfunction and ultimately neuronal death. This work identifies an essential mechanism in amyloid \u03b2 neurotoxicity and explains many of the observed postsynaptic alterations.\n                  <\/jats:p>\n                <\/jats:sec>\n                <jats:sec>\n                  <jats:title>Highlights<\/jats:title>\n                  <jats:p>\n                    <jats:bold>\n                      Immediate effects of A\u03b2-induced stimulation of \u03b2\n                      <jats:sub>2<\/jats:sub>\n                      AR on Cav1.2:\n                    <\/jats:bold>\n                  <\/jats:p>\n                  <jats:list list-type=\"bullet\">\n                    <jats:list-item>\n                      <jats:p>A\u03b2 induces phosphorylation of Cav1.2 on S1928 by PKA<\/jats:p>\n                    <\/jats:list-item>\n                    <jats:list-item>\n                      <jats:p>\n                        A\u03b2 augments Cav1.2 activity via \u03b2\n                        <jats:sub>2<\/jats:sub>\n                        AR-induced S1928 phosphorylation within seconds\n                      <\/jats:p>\n                    <\/jats:list-item>\n                  <\/jats:list>\n                  <jats:p>\n                    <jats:bold>\n                      A\u03b2-induced \u03b2\n                      <jats:sub>2<\/jats:sub>\n                      AR - Cav1.2 signaling has the following synaptotoxic effects.\n                    <\/jats:bold>\n                  <\/jats:p>\n                  <jats:list list-type=\"bullet\">\n                    <jats:list-item>\n                      <jats:p>\n                        A\u03b2 induces postsynaptic accumulation of Ca-permeable AMPARs via \u03b2\n                        <jats:sub>2<\/jats:sub>\n                        AR - Cav1.2 signaling within 20 min\n                      <\/jats:p>\n                    <\/jats:list-item>\n                    <jats:list-item>\n                      <jats:p>\n                        A\u03b2 impairs long-term potentiation (LTP) via \u03b2\n                        <jats:sub>2<\/jats:sub>\n                        AR - Cav1.2 signaling\n                      <\/jats:p>\n                    <\/jats:list-item>\n                    <jats:list-item>\n                      <jats:p>A\u03b2 impairs postsynaptic structure and neuronal viability over 24 h<\/jats:p>\n                    <\/jats:list-item>\n                    <jats:list-item>\n                      <jats:p>\n                        Potency of A\u03b2 in\n                        <jats:underline>all<\/jats:underline>\n                        the above effects is very high (100 nM A\u03b2 is saturating!)\n                      <\/jats:p>\n                    <\/jats:list-item>\n                    <jats:list-item>\n                      <jats:p>\n                        <jats:underline>All<\/jats:underline>\n                        effects are prevented in S1928A KI mice and acute displaces \u03b2\n                        <jats:sub>2<\/jats:sub>\n                        AR from Cav1.2 with tat-Pep\n                        <jats:sub>1923<\/jats:sub>\n                      <\/jats:p>\n                    <\/jats:list-item>\n                  <\/jats:list>\n                <\/jats:sec>","DOI":"10.64898\/2026.04.25.720803","type":"posted-content","created":{"date-parts":[[2026,4,30]],"date-time":"2026-04-30T01:09:08Z","timestamp":1777511348000},"source":"Crossref","is-referenced-by-count":1,"title":["A Unifying Mechanism for Synaptic Amyloid \u03b2 Toxicity \u03b2 Adrenergic Potentiation of the Ca\n                  <sup>2+<\/sup>\n                  Channel CaV1.2 by Amyloid \u03b2"],"prefix":"10.64898","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5852-1835","authenticated-orcid":false,"given":"Peter","family":"Bartels","sequence":"first","affiliation":[{"name":"Department of Pharmacology, University of California Davis, CA 95616-8636, 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