Evidence map›Paper›PMID 27474409›Full record

ArticleThe Biochemical journal2016

Inositol hexakisphosphate kinase 1 (IP6K1) activity is required for cytoplasmic dynein-driven transport.

Manasa Chanduri, Ashim Rai, Aushaq Bashir Malla, Mingxuan Wu, Dorothea Fiedler, Roop Mallik, Rashna Bhandari

Open access · hybridAbstract read
In one paragraph

Article in The Biochemical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

44 citing papers in PubMed, 72 citations in OpenAlex.

  1. Review
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  4. The inositol pyrophosphate 5-InsPThe Journal of biological chemistry · 2026
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  18. Whole BodyInternational journal of molecular sciences · 2022
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Manasa ChanduriLaboratory of Cell Signalling, Centre for DNA Fingerprinting and Diagnostics, Nampally, Hyderabad 500001, India Graduate Studies, Manipal University, Manipal, India.
Ashim RaiDepartment of Biological Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Mumbai 400005, India.
Aushaq Bashir MallaLaboratory of Cell Signalling, Centre for DNA Fingerprinting and Diagnostics, Nampally, Hyderabad 500001, India Graduate Studies, Manipal University, Manipal, India.
Mingxuan WuDepartment of Chemistry, Princeton University, Washington Rd, Princeton, NJ 08544, U.S.A.
Dorothea FiedlerDepartment of Chemistry, Princeton University, Washington Rd, Princeton, NJ 08544, U.S.A.
Roop MallikDepartment of Biological Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Mumbai 400005, India.
Rashna BhandariLaboratory of Cell Signalling, Centre for DNA Fingerprinting and Diagnostics, Nampally, Hyderabad 500001, India.
Centre for DNA Fingerprinting and Diagnostics · INTata Institute of Fundamental Research · IN

Funding

Wellcome Trust IA/S/11/2500255Wellcome Trust WT079214MAWellcome Trust-DBT India Alliance 500020/Z/09/Z
6 · The paper itself

Abstract

Inositol pyrophosphates, such as diphosphoinositol pentakisphosphate (IP7), are conserved eukaryotic signaling molecules that possess pyrophosphate and monophosphate moieties. Generated predominantly by inositol hexakisphosphate kinases (IP6Ks), inositol pyrophosphates can modulate protein function by posttranslational serine pyrophosphorylation. Here, we report inositol pyrophosphates as novel regulators of cytoplasmic dynein-driven vesicle transport. Mammalian cells lacking IP6K1 display defects in dynein-dependent trafficking pathways, including endosomal sorting, vesicle movement, and Golgi maintenance. Expression of catalytically active but not inactive IP6K1 reverses these defects, suggesting a role for inositol pyrophosphates in these processes. Endosomes derived from slime mold lacking inositol pyrophosphates also display reduced dynein-directed microtubule transport. We demonstrate that Ser51 in the dynein intermediate chain (IC) is a target for pyrophosphorylation by IP7, and this modification promotes the interaction of the IC N-terminus with the p150(Glued) subunit of dynactin. IC-p150(Glued) interaction is decreased, and IC recruitment to membranes is reduced in cells lacking IP6K1. Our study provides the first evidence for the involvement of IP6Ks in dynein function and proposes that inositol pyrophosphate-mediated pyrophosphorylation may act as a regulatory signal to enhance dynein-driven transport.

Indexed as

AnimalsCytoplasmDyneinsEndosomesFemaleGolgi ApparatusHumansInositol PhosphatesMicePhosphorylationPhosphotransferases (Phosphate Group Acceptor)Protein TransportDyneinsIhpk1 protein, mouseInositol PhosphatesIP6K1 protein, humanPhosphotransferases (Phosphate Group Acceptor)dynactindyneininositol hexakisphosphate kinase 1inositol pyrophosphatesprotein pyrophosphorylation

Identifiers

PMID27474409
PMCPMC5095903
OpenAlexW2502710244

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.