ArticleThe Journal of biological chemistry2003
Association of kinesin light chain with outer dense fibers in a microtubule-independent fashion.
Article in The Journal of biological chemistry, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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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.
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Who cites it
11 citing papers in PubMed, 32 citations in OpenAlex.
- Insights on Human Small Heat Shock Proteins and Their Alterations in Diseases.Frontiers in molecular biosciences · 2022Review
- Improving the overall survival prognosis prediction accuracy: A 9-gene signature in CRC patients.Cancer medicine · 2021Article
- Article
- Analysis of the function of KIF3A and KIF3B in the spermatogenesis in Boleophthalmus pectinirostris.Fish physiology and biochemistry · 2018Article
- Altered expression of KLC3 may affect semen parameters.International journal of reproductive biomedicine · 2016Article
- Functional Analysis of KIF3A and KIF3B during Spermiogenesis of Chinese Mitten Crab Eriocheir sinensis.PloS one · 2014Article
- Article
- The small heat shock protein ODF1/HSPB10 is essential for tight linkage of sperm head to tail and male fertility in mice.Molecular and cellular biology · 2012Article
- Ornithine decarboxylase antizyme Oaz3 modulates protein phosphatase activity.The Journal of biological chemistry · 2011Article
- Mammalian transcription in support of hybrid mRNA and protein synthesis in testis and lung.The Journal of biological chemistry · 2006Article
- Rat kinesin light chain 3 associates with spermatid mitochondria.Developmental biology · 2004Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Conventional kinesin I motor molecules are heterotetramers consisting of two kinesin light chains (KLCs) and two kinesin heavy chains. The interaction between the heavy and light chains is mediated by the KLC heptad repeat (HR), a leucine zipper-like motif. Kinesins bind to microtubules and are involved in various cellular functions, including transport and cell division. We recently isolated a novel KLC gene, klc3. klc3 is the only known KLC expressed in post-meiotic male germ cells. A monoclonal anti-KLC3 antibody was developed that, in immunoelectron microscopy, detects KLC3 protein associated with outer dense fibers (ODFs), unique structural components of sperm tails. No significant binding of KLC3 with microtubules was observed with this monoclonal antibody. In vitro experiments showed that KLC3-ODF binding occurred in the absence of kinesin heavy chains or microtubules and required the KLC3 HR. ODF1, a major ODF protein, was identified as the KLC3 binding partner. The ODF1 leucine zipper and the KLC3 HR mediated the interaction. These results identify and characterize a novel interaction between a KLC and a non-microtubule macromolecular structure and suggest that KLC3 could play a microtubule-independent role during formation of sperm tails.
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Registered trials
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.