Proteomics

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Structural architecture and function of the human NALCN channelosome

ABSTRACT: Chemical cross-linking coupled to mass spectrometry was used to study the subunit organization of the NALCN channelosome consisting of the proteins NALCN, FAM155A, UNC79 and UNC80. Cross-linking data was generated using the reagents disuccinimidyl suberate (DSS), pimelic dihydrazide (PDH), and 4-(4,6-Dimethoxy-1,3,5-triazin-2-yl)-4-methylmorpholinium (DMTMM) chloride, and was analyzed in combination with data from cryo-electron microscopy.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Alexander Leitner  

LAB HEAD: Alexander Leitner

PROVIDER: PXD027213 | Pride | 2021-11-23

REPOSITORIES: Pride

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210308_LU02_aleitner_NALCN_01.raw Raw
210308_LU02_aleitner_NALCN_02.raw Raw
210308_LU02_aleitner_NALCN_03.raw Raw
210308_LU02_aleitner_NALCN_04.raw Raw
210308_LU02_aleitner_NALCN_05.raw Raw
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Publications

Depolarizing sodium (Na<sup>+</sup>) leak currents carried by the NALCN channel regulate the resting membrane potential of many neurons to modulate respiration, circadian rhythm, locomotion and pain sensitivity<sup>1-8</sup>. NALCN requires FAM155A, UNC79 and UNC80 to function, but the role of these auxiliary subunits is not understood<sup>3,7,9-12</sup>. NALCN, UNC79 and UNC80 are essential in rodents<sup>2,9,13</sup>, and mutations in human NALCN and UNC80 cause severe developmental and neurol  ...[more]

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