Cited by 36Light effects on plantsPhotosynthetic Processes and MechanismsPlant Molecular Biology Research

The kinesin‐like proteins, KAC1/2, regulate actin dynamics underlying chloroplast light‐avoidance in Physcomitrella patens

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Shen, Zhiyuan, Liu, Yen‐Chen, Bibeau, Jeffrey P., Lemoi, Kyle P., Tüzel, Erkan, Vidali, Luis·2015·Journal of Integrative Plant Biology

Abstract

In plants, light determines chloroplast position; these organelles show avoidance and accumulation responses in high and low fluence‐rate light, respectively. Chloroplast motility in response to light is driven by cytoskeletal elements. The actin cytoskeleton mediates chloroplast photorelocation responses in Arabidopsis thaliana. In contrast, in the moss Physcomitrella patens, both, actin filaments and microtubules can transport chloroplasts. Because of the surprising evidence that two kinesin‐like proteins (called KACs) are important for actin‐dependent chloroplast photorelocation in vascular plants, we wanted to determine the cytoskeletal system responsible for the function of these proteins in moss. We performed gene‐specific silencing using RNA interference in P. patens. We confirmed existing reports using gene knockouts, that PpKAC1 and PpKAC2 are required for chloroplast dispersion under uniform white light conditions, and that the two proteins are functionally equivalent. To address the specific cytoskeletal elements responsible for motility, this loss‐of‐function approach was combined with cytoskeleton‐targeted drug studies. We found that, in P. patens, these KACs mediate the chloroplast light‐avoidance response in an actin filament‐dependent, rather than a microtubule‐dependent manner. Using correlation‐decay analysis of cytoskeletal dynamics, we found that PpKAC stabilizes cortical actin filaments, but has no effect on microtubule dynamics.

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Crossref · 10.1111/jipb.12303

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  • The kac1 kac2 double mutant plant did not contain CP-actin filaments, and chloroplasts were shed from the plasma membrane.

    “The kac1 kac2 double mutant plant did not contain CP-actin filaments, and chloroplasts were shed from the plasma membrane”

    From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Shen et al., 2015

    The Introduction (page unavailable) reports that a KAC1/KAC2 double knockout causes chloroplasts to cluster in the center of moss cells, consistent with a role in anchoring them to the plasma membrane. The Results (page unavailable) confirm clustering in double-knockdown plants. Neither passage establishes that chloroplasts were shed from the membrane, and the paper does not report that CP-actin filaments were absent. (LLM, conf=0.86)

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Cited by

Authors
Shen, Z., Liu, Y., Bibeau, J. P., Lemoi, K. P., Tüzel, E., & Vidali, L.
Affiliations
Worcester Polytechnic Institute (US)
Corresponding author
Vidali, Luis
Venue
Journal of Integrative Plant Biology
Publisher
Wiley
Published
2015-01
Volume
57
Issue
1
Pages
106-119
ISSN
  • 0577-7496 (ISSN-L)
  • 1672-9072
  • 1744-7909
OpenAlex
W1511601658
Cited by
36
References
52
Citations by year
2026: 1 · 2025: 4 · 2024: 2 · 2023: 2 · 2022: 4 · 2021: 1 · 2020: 3 · 2019: 1 · 2018: 8 · 2017: 4 · 2016: 3 · 2015: 1 · 2014: 2
FWCI
3.89
Type
journal article
Language
en
Open access
Locations
  • Journal of Integrative Plant Biology (publishedVersion)
  • PubMed (publishedVersion)
Funders
Eppley Foundation for Research
Topics
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Light effects on plants
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
Keywords
kinesin-like protein, actin cytoskeleton, microtubules, cortical actin filaments, actin dynamics, bryophytes, Physcomitrella patens
MeSH terms
Actins, Chloroplasts, Light, Actin Cytoskeleton, Microtubules, Movement, Plant Proteins, Kinesins, Bryopsida, Gene Knockdown Techniques

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