An ankyrin G–binding motif mediates TRAAK periodic localization at axon initial segments of hippocampal pyramidal neurons
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An ankyrin G–binding motif mediates TRAAK periodic localization at axon initial segments of hippocampal pyramidal neurons. / Luque-Fernández, Virginia; Vanspauwen, Sam K.; Landra-Willm, Arnaud; Arvedsen, Emil; Besquent, Maïlys; Rasmussen, Hanne B.; Sandoz, Guillaume.
I: Proceedings of the National Academy of Sciences of the United States of America, Bind 121, Nr. 31, e2310120121, 2024.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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T1 - An ankyrin G–binding motif mediates TRAAK periodic localization at axon initial segments of hippocampal pyramidal neurons
AU - Luque-Fernández, Virginia
AU - Vanspauwen, Sam K.
AU - Landra-Willm, Arnaud
AU - Arvedsen, Emil
AU - Besquent, Maïlys
AU - Rasmussen, Hanne B.
AU - Sandoz, Guillaume
N1 - Publisher Copyright: Copyright © 2024 the Author(s).
PY - 2024
Y1 - 2024
N2 - The axon initial segment (AIS) is a critical compartment in neurons. It converts post-synaptic input into action potentials that subsequently trigger information transfer to target neurons. This process relies on the presence of several voltage-gated sodium (NaV) and potassium (KV) channels that accumulate in high densities at the AIS. TRAAK is a mechanosensitive leak potassium channel that was recently localized to the nodes of Ranvier. Here, we uncover that TRAAK is also present in AISs of hippocampal and cortical neurons in the adult rat brain as well as in AISs of cultured rat hippocampal neurons. We show that the AIS localization is driven by a C-terminal ankyrin G–binding sequence that organizes TRAAK in a 190 nm spaced periodic pattern that codistributes with periodically organized ankyrin G. We furthermore uncover that while the identified ankyrin G–binding motif is analogous to known ankyrin G–binding motifs in NaV1 and KV7.2/KV7.3 channels, it was acquired by convergent evolution. Our findings identify TRAAK as an AIS ion channel that convergently acquired an ankyrin G–binding motif and expand the role of ankyrin G to include the nanoscale organization of ion channels at the AIS.
AB - The axon initial segment (AIS) is a critical compartment in neurons. It converts post-synaptic input into action potentials that subsequently trigger information transfer to target neurons. This process relies on the presence of several voltage-gated sodium (NaV) and potassium (KV) channels that accumulate in high densities at the AIS. TRAAK is a mechanosensitive leak potassium channel that was recently localized to the nodes of Ranvier. Here, we uncover that TRAAK is also present in AISs of hippocampal and cortical neurons in the adult rat brain as well as in AISs of cultured rat hippocampal neurons. We show that the AIS localization is driven by a C-terminal ankyrin G–binding sequence that organizes TRAAK in a 190 nm spaced periodic pattern that codistributes with periodically organized ankyrin G. We furthermore uncover that while the identified ankyrin G–binding motif is analogous to known ankyrin G–binding motifs in NaV1 and KV7.2/KV7.3 channels, it was acquired by convergent evolution. Our findings identify TRAAK as an AIS ion channel that convergently acquired an ankyrin G–binding motif and expand the role of ankyrin G to include the nanoscale organization of ion channels at the AIS.
KW - ankyrin G
KW - axon initial segment
KW - K2P4.1
KW - KCNK4
KW - STED
U2 - 10.1073/pnas.2310120121
DO - 10.1073/pnas.2310120121
M3 - Journal article
C2 - 39058579
AN - SCOPUS:85199723948
VL - 121
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
SN - 0027-8424
IS - 31
M1 - e2310120121
ER -
ID: 402321853