Phylogenetic Analysis of the Kinesin Superfamily from Physcomitrella
Open accessAbstract
Kinesins are an ancient superfamily of microtubule dependent motors. They participate in an extensive and diverse list of essential cellular functions, including mitosis, cytokinesis, cell polarization, cell elongation, flagellar development, and intracellular transport. Based on phylogenetic relationships, the kinesin superfamily has been subdivided into 14 families, which are represented in most eukaryotic phyla. The functions of these families are sometimes conserved between species, but important variations in function across species have been observed. Plants possess most kinesin families including a few plant specific families. With the availability of an ever increasing number of genome sequences from plants, it is important to document the complete complement of kinesins present in a given organism. This will help develop a molecular framework to explore the function of each family using genetics, biochemistry, and cell biology. The moss Physcomitrella patens has emerged as a powerful model organism to study gene function in plants, which makes it a key candidate to explore complex gene families, such as the kinesin superfamily. Here we report a detailed phylogenetic characterization of the 71 kinesins of the kinesin superfamily in Physcomitrella. We found a remarkable conservation of families and subfamily classes with Arabidopsis, which is important for future comparative analysis of function. Some of the families, such as kinesins 14s are composed of fewer members in moss, while other families, such as the kinesin 12s are greatly expanded. To improve the comparison between species, and to simplify communication between research groups, we propose a classification of subfamilies based on our phylogenetic analysis.
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The FERM domain likely serves as the cargo-binding domain.
“likely serving as the cargo‐binding domain”
From <scp>RNAi</scp> reveals a unique set of kinesins mediating chloroplast motility in the giant cytoplasm of <i>Bryopsis</i> (Ulvophyceae), a coenocytic green alga (2026) · cites this paper as Shen et al., 2012
In Results and Discussion > Kinesin 14 (page unavailable), the paper describes the FERM domains as binding microtubules and infers that the moss kinesins likely cross-link or bundle microtubules. It does not describe FERM as a cargo-binding domain; it proposes a different role instead. (LLM, conf=0.84)
Checked by a reasoning model — may be wrong.
Experimental — accuracy not yet measuredKin14II in land plants generally has the CH domain in its tail.
“Kin14II in land plants generally has the calponin homology (CH) domain in its tail (Shen et al., 2012)”
From <scp>RNAi</scp> reveals a unique set of kinesins mediating chloroplast motility in the giant cytoplasm of <i>Bryopsis</i> (Ulvophyceae), a coenocytic green alga (2026) · cites this paper as Shen et al., 2012
The Results and Discussion section on kinesin 14 reports CH domains in all four Physcomitrella class II members and in ATK4 and its cotton and rice homologs. This supports the pattern across several land plants, but the text does not establish that Kin14II generally has the domain across land plants or explicitly locate it in the tail. (LLM, conf=0.84)
Experimental — accuracy not yet measuredCanonical Kin14VIs (KCBPs) contain MYTH4 and FERM domains in the tail region.
“Canonical Kin14VIs (KCBPs) contain MYTH4 and FERM domains in the tail region”
From <scp>RNAi</scp> reveals a unique set of kinesins mediating chloroplast motility in the giant cytoplasm of <i>Bryopsis</i> (Ulvophyceae), a coenocytic green alga (2026) · cites this paper as Shen et al., 2012
The Results and Discussion (Kinesin 14; page unavailable) identifies KCBP as the Arabidopsis member of class VI and says its four moss homologs contain MyTH4 and two FERM domains. It does not establish that canonical KCBPs generally contain those domains or explicitly place them in the tail region. (LLM, conf=0.85)
Experimental — accuracy not yet measuredThe FERM domain is essential for chloroplast motility.
“the FERM domain is essential for chloroplast motility”
From <scp>RNAi</scp> reveals a unique set of kinesins mediating chloroplast motility in the giant cytoplasm of <i>Bryopsis</i> (Ulvophyceae), a coenocytic green alga (2026) · cites this paper as Shen et al., 2012
In Results and Discussion > Kinesin 14 (page unavailable), the paper describes FERM domains as binding microtubules and suggests that the moss kinesins containing them may bundle microtubules. Its separate discussion of chloroplast movement concerns KAC1 and KAC2 and does not say that a FERM domain is essential for that movement. Searched for the claimed FERM–chloroplast connection. (LLM, conf=0.76)
Experimental — accuracy not yet measured
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- Authors
- Shen, Z., Collatos, A. R., Bibeau, J. P., Furt, F., & Vidali, L.
- Affiliations
- Worcester Polytechnic Institute (US)
- Corresponding author
- Vidali, Luis
- Venue
- Frontiers in Plant Science
- Publisher
- Frontiers Media SA
- Published
- 2012
- Volume
- 3
- Pages
- 230-230
- ISSN
- 1664-462X (ISSN-L)
- PMC
- PMC3472504
- OpenAlex
- W2005767543
- Cited by
- 60
- References
- 85
- Citations by year
- 2026: 2 · 2025: 7 · 2024: 6 · 2023: 4 · 2022: 6 · 2021: 2 · 2020: 4 · 2019: 3 · 2018: 7 · 2017: 4 · 2016: 3 · 2015: 6 · 2014: 5 · 2013: 1
- FWCI
- 1.82
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Frontiers in Plant Science (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Science Foundation (1002837)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Chromosomal and Genetic Variations
- Keywords
- kinesin superfamily, Physcomitrella patens, bryophytes, kinesin-12, kinesin-14, Arabidopsis comparison, gene family evolution
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