Evidence map›Paper›PMID 18361505›Full record

ArticleBiochemistry2008

Conventional kinesin holoenzymes are composed of heavy and light chain homodimers.

Scott R DeBoer, YiMei You, Anita Szodorai, Agnieszka Kaminska, Gustavo Pigino, Evelyn Nwabuisi, Bin Wang, Tatiana Estrada-Hernandez, Stefan Kins, Scott T Brady and 1 more

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

55 citing papers in PubMed, 79 citations in OpenAlex.

  1. Review
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  9. Tau phosphorylation and PAD exposure in regulation of axonal growth.Frontiers in cell and developmental biology · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Tau and Axonal Transport Misregulation in Tauopathies.Advances in experimental medicine and biology · 2019
    Review
  15. Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. BORC/kinesin-1 ensemble drives polarized transport of lysosomes into the axon.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 2 institutions in 2 countries.

Scott R DeBoerDepartment of Anatomy and Cell Biology, University of Illinois at Chicago, Chicago, Illinois 60612, USA.
YiMei You
Anita Szodorai
Agnieszka Kaminska
Gustavo Pigino
Evelyn Nwabuisi
Bin Wang
Tatiana Estrada-Hernandez
Stefan Kins
Scott T Brady
Gerardo Morfini
Heidelberg University · DEUniversity of Illinois Chicago · US

Funding

MOLECULAR MECHANISMS OF AXONAL TRANSPORTR01NS023868 · NINDS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI BRADY, SCOTT THOMAS · 1986 to 2010
$3.7M
APO E Receptors and Modulation of Fast Axonal TransportR01NS043408 · NINDS · UT SOUTHWESTERN MEDICAL CENTER · PI HERZ, JOACHIM J · 2002 to 2006
$1.8M
REGULATION OF FAST AXONAL TRANSPORT DIABETIC NEUROPATHYR01NS041170 · NINDS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI BRADY, SCOTT THOMAS · 2000 to 2004
$1.6M
PROPERTIES OF AXONAL TUBULIN RELATED TO NEURONAL GROWTHR01NS023320 · NINDS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI BRADY, SCOTT THOMAS · 1985 to 2003
$1.0M
Molecular Mechanisms of Axonal TransportR56NS023868 · NINDS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI BRADY, SCOTT THOMAS · 2011 to 2011
$554k
NINDS NIH HHS NS23320NINDS NIH HHS NS23868NINDS NIH HHS NS41170NINDS NIH HHS NS43408NINDS NIH HHS R01 NS023320NINDS NIH HHS R01 NS023868NINDS NIH HHS R01 NS041170NINDS NIH HHS R01 NS043408NINDS NIH HHS R56 NS023868
6 · The paper itself

Abstract

Conventional kinesin is a major microtubule-based motor protein responsible for anterograde transport of various membrane-bounded organelles (MBO) along axons. Structurally, this molecular motor protein is a tetrameric complex composed of two heavy (kinesin-1) chains and two light chain (KLC) subunits. The products of three kinesin-1 (kinesin-1A, -1B, and -1C, formerly KIF5A, -B, and -C) and two KLC (KLC1, KLC2) genes are expressed in mammalian nervous tissue, but the functional significance of this subunit heterogeneity remains unknown. In this work, we examine all possible combinations among conventional kinesin subunits in brain tissue. In sharp contrast with previous reports, immunoprecipitation experiments here demonstrate that conventional kinesin holoenzymes are formed of kinesin-1 homodimers. Similar experiments confirmed previous findings of KLC homodimerization. Additionally, no specificity was found in the interaction between kinesin-1s and KLCs, suggesting the existence of six variant forms of conventional kinesin, as defined by their gene product composition. Subcellular fractionation studies indicate that such variants associate with biochemically different MBOs and further suggest a role of kinesin-1s in the targeting of conventional kinesin holoenzymes to specific MBO cargoes. Taken together, our data address the combination of subunits that characterize endogenous conventional kinesin. Findings on the composition and subunit organization of conventional kinesin as described here provide a molecular basis for the regulation of axonal transport and delivery of selected MBOs to discrete subcellular locations.

Indexed as

AnimalsAntibodiesDimerizationHoloenzymesIntracellular MembranesKinesinsMiceMicrosomesProtein SubunitsAntibodiesHoloenzymesKinesinsKlc2 protein, mouseKns2 protein, mouseProtein Subunits

Identifiers

PMID18361505
PMCPMC2644488
OpenAlexW2091035365

What OpenQuestion holds

Textmetadata
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.