Evidence map›Paper›PMID 29093024›Full record

ArticleMolecular biology of the cell2017

Phosphorylation of multiple sites within an acidic region of Alcadein α is required for kinesin-1 association and Golgi exit of Alcadein α cargo.

Yuriko Sobu, Keiko Furukori, Kyoko Chiba, Angus C Nairn, Masataka Kinjo, Saori Hata, Toshiharu Suzuki

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.9field-weighted citation impact, top 28% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

10 citing papers in PubMed, 17 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

Yuriko SobuLaboratory of Neuroscience, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.
Keiko FurukoriLaboratory of Neuroscience, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.
Kyoko ChibaLaboratory of Neuroscience, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.
Angus C NairnDepartment of Psychiatry, Yale University School of Medicine, New Haven, CT 06508.
Masataka KinjoLaboratory of Molecular Cell Dynamics, Faculty of Advanced Life Science, Hokkaido University, Sapporo, 001-0021, Japan.
Saori HataLaboratory of Neuroscience, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.
Toshiharu SuzukiLaboratory of Neuroscience, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan tsuzuki@pharm.hokudai.ac.jp.
Hokkaido University · JPYale University · US

Funding

Yale Alzheimer Disease Research CenterP50AG047270 · NIA · YALE UNIVERSITY · PI MAROTTOLI, RICHARD · 2015 to 2019
$8.3M
NIA NIH HHS P50 AG047270
6 · The paper itself

Abstract

Alcadein α (Alcα) is a major cargo of kinesin-1 that is subjected to anterograde transport in neuronal axons. Two tryptophan- and aspartic acid-containing (WD) motifs located in its cytoplasmic domain directly bind the tetratricopeptide repeat (TPR) motifs of the kinesin light chain (KLC), which activate kinesin-1 and recruit kinesin-1 to Alcα cargo. We found that phosphorylation of three serine residues in the acidic region located between the two WD motifs is required for interaction with KLC. Phosphorylation of these serine residues may alter the disordered structure of the acidic region to induce direct association with KLC. Replacement of these serines with Ala results in a mutant that is unable to bind kinesin-1, which impairs exit of Alcα cargo from the Golgi. Despite this deficiency, the compromised Alcα mutant was still transported, albeit improperly by vesicles following missorting of the Alcα mutant with amyloid β-protein precursor (APP) cargo. This suggests that APP partially compensates for defective Alcα in anterograde transport by providing an alternative cargo receptor for kinesin-1.

Indexed as

Adaptor Proteins, Signal TransducingAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAnimalsAxonal TransportBiological TransportCalcium-Binding ProteinsGolgi ApparatusHEK293 CellsHumansKinesinsMiceMice, Inbred C57BLMicrotubule-Associated ProteinsPhosphorylationProtein DomainsAdaptor Proteins, Signal TransducingAmyloid beta-PeptidesAmyloid beta-Protein PrecursorCalcium-Binding ProteinsCLSTN1 protein, humanClstn1 protein, mouseKIF5B protein, humanKinesinsMicrotubule-Associated Proteins

Identifiers

PMID29093024
PMCPMC5739299
OpenAlexW2766537734

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.