ArticlePlanta2004
Localization of two homologous Arabidopsis kinesin-related proteins in the phragmoplast.
Article in Planta, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 47 citations in OpenAlex.
- A Rab/Kinesin-12/kinase module couples vesicle delivery and phragmoplast dynamics during plant cell cytokinesis.The EMBO journal · 2026Article
- Cellular dynamics and molecular signaling networks of plant cytokinesis.Molecules and cells · 2026Review
- The OPAQUE1/DISCORDIA2 myosin XI is required for phragmoplast guidance during asymmetric cell division in maize.The Plant cell · 2023Article
- Novel inhibitors of microtubule organization and phragmoplast formation in diverse plant species.Life science alliance · 2023Article
- The localization of PHRAGMOPLAST ORIENTING KINESIN1 at the division site depends on the microtubule-binding proteins TANGLED1 and AUXIN-INDUCED IN ROOT CULTURES9 in Arabidopsis.The Plant cell · 2022Article
- KINESIN-12E regulates metaphase spindle flux and helps control spindle size in Arabidopsis.The Plant cell · 2021Article
- The functions of kinesin and kinesin-related proteins in eukaryotes.Cell adhesion & migration · 2020Review
- Plant Kinesin-12: Localization Heterogeneity and Functional Implications.International journal of molecular sciences · 2019Review
- Dual localized kinesin-12 POK2 plays multiple roles during cell division and interacts with MAP65-3.EMBO reports · 2018Article
- Kinesins and Myosins: Molecular Motors that Coordinate Cellular Functions in Plants.Annual review of plant biology · 2018Review
- Phragmoplast microtubule dynamics - a game of zones.Journal of cell science · 2018Review
- Characterization and expression profiling of cucumber kinesin genes during early fruit development: revealing the roles of kinesins in exponential cell production and enlargement in cucumber fruit.Journal of experimental botany · 2013Article
- Functions of the Arabidopsis kinesin superfamily of microtubule-based motor proteins.Protoplasma · 2012Review
- Arabidopsis microtubule-associated protein MAP65-3 cross-links antiparallel microtubules toward their plus ends in the phragmoplast via its distinct C-terminal microtubule binding domain.The Plant cell · 2012Article
- Phylogenetic analysis of the Kinesin superfamily from physcomitrella.Frontiers in plant science · 2012Article
- Interaction of antiparallel microtubules in the phragmoplast is mediated by the microtubule-associated protein MAP65-3 in Arabidopsis.The Plant cell · 2011Article
- Evaluating the microtubule cytoskeleton and its interacting proteins in monocots by mining the rice genome.Annals of botany · 2009Review
- Two Arabidopsis phragmoplast-associated kinesins play a critical role in cytokinesis during male gametogenesis.The Plant cell · 2007Article
- Coiled-coil protein composition of 22 proteomes--differences and common themes in subcellular infrastructure and traffic control.BMC evolutionary biology · 2005Article
- Midbodies and phragmoplasts: analogous structures involved in cytokinesis.Trends in cell biology · 2005Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
During plant cytokinesis, kinesin-related motor proteins are believed to play critical roles in microtubule organization and vesicle transport in the phragmoplast. Previously, we reported that the motor AtPAKRP1 was associated with the plus end of phragmoplast microtubules in Arabidopsis thaliana [Lee Y-RJ, Liu B (2000) Curr Biol 10:797-800]. In this paper, we report a full-length cDNA from the same organism, which encodes a polypeptide 74% identical to AtPAKRP1. This AtPAKRP1-like protein--AtPAKRP1L--and AtPAKRP1 share similar domain structures along the polypeptides. Peptide antibodies were raised and purified to distinguish the two polypeptides in vitro and in vivo. When monospecific anti-AtPAKRP1 and anti-AtPAKRP1L antibodies were used in immunofluorescence, they both decorated the plus end of phragmoplast microtubules at all stages of phragmoplast development. Their localization patterns were indistinguishable from each other. By using bacterially expressed fusion proteins of motor-less versions of both polypeptides, it was revealed that AtPAKRP1 and AtPAKRP1L were able to interact with themselves and with each other. Using T-DNA insertional mutants, it was also demonstrated that AtPAKRP1 and AtPAKRP1L were not required for each other's localization. Our results therefore indicate that AtPAKRP1 and AtPAKRP1L are both expressed in the same cells, and likely have identical functions in the phragmoplast by forming either homodimers or heterodimers.
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Registered trials
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