Proteomics

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ATP-Citrate lyase fuels axonal transport across species


ABSTRACT: Microtubule (MT)-based transport is an evolutionary conserved processed finely tuned by posttranslational modifications. Among them, tubulin acetylation, which is catalyzed by the α-tubulin N-acetyltransferase 1, Atat1, facilitates the recruitment and processivity of molecular motors along MT tracks. However, the mechanisms that controls Atat1 activity remains poorly understood. Here we show that a pool of vesicular ATP-citrate lyase Acly acts as a rate limiting enzyme to modulate Atat1 activity by controlling availability of Acetyl-CoA. In addition, we showed that Acly expression is reduced upon loss of Elongator activity, further connecting Elongator to Atat1 in the pathway regulating -tubulin acetylation and MT-dependent transport in projection neurons across species. Remarkably, comparable defects occur in fibroblasts from Familial Dysautonomia (FD) patients bearing an autosomal recessive mutation in the gene coding for the Elongator subunit ELP1. Our data may thus shine new light on the pathophysiological mechanisms underlying FD.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Mus Musculus (mouse)

SUBMITTER: Tamar Ziv  

LAB HEAD: Miguel Weil

PROVIDER: PXD021186 | Pride | 2022-02-16

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
44780txt.zip Other
Seq44781_QE2.raw Raw
Seq44782_QE2.raw Raw
Seq44783_QE2.raw Raw
Seq44784_QE2.raw Raw
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Publications


Microtubule (MT)-based transport is an evolutionary conserved process finely tuned by posttranslational modifications. Among them, α-tubulin acetylation, primarily catalyzed by a vesicular pool of α-tubulin N-acetyltransferase 1 (Atat1), promotes the recruitment and processivity of molecular motors along MT tracks. However, the mechanism that controls Atat1 activity remains poorly understood. Here, we show that ATP-citrate lyase (Acly) is enriched in vesicles and provide Acetyl-Coenzyme-A (Acety  ...[more]

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