Plant myosins

T. Shimmen; R. W. Ridge; I. Lambiris; J. Plazinski; E. Yokota; R. E. Williamson

doi:10.1007/BF02524256

Plant myosins

T. Shimmen^*, R. W. Ridge, I. Lambiris, J. Plazinski, E. Yokota, R. E. Williamson

^*Corresponding author for this work

Research output: Contribution to journal › Review article › peer-review

25 Citations (Scopus)

Abstract

Plant myosins are motor proteins that bind to the external surfaces of organelles and interact with the cytoskeletal protein actin (as actin microfilaments), which organizes and directs intracellular movement. Recent progress in physiological, biochemical, immunological, and genetical studies of plant myosin has revealed considerable information about the structures and functions of these important molecules. This article briefly reviews the history of plant myosin research, summarizes recent progress, and highlights directions for future research.

Original language	English
Pages (from-to)	1-10
Number of pages	10
Journal	Protoplasma
Volume	214
Issue number	1-2
DOIs	https://doi.org/10.1007/BF02524256
Publication status	Published - 2000

Access to Document

10.1007/BF02524256

Cite this

@article{944894113de9466e901facf85e07cd56,

title = "Plant myosins",

abstract = "Plant myosins are motor proteins that bind to the external surfaces of organelles and interact with the cytoskeletal protein actin (as actin microfilaments), which organizes and directs intracellular movement. Recent progress in physiological, biochemical, immunological, and genetical studies of plant myosin has revealed considerable information about the structures and functions of these important molecules. This article briefly reviews the history of plant myosin research, summarizes recent progress, and highlights directions for future research.",

keywords = "Actin filament, Ca, Calmodulin, Cytoplasmic streaming, Myosin, Phosphorylation",

author = "T. Shimmen and Ridge, {R. W.} and I. Lambiris and J. Plazinski and E. Yokota and Williamson, {R. E.}",

year = "2000",

doi = "10.1007/BF02524256",

language = "English",

volume = "214",

pages = "1--10",

journal = "Protoplasma",

issn = "0033-183X",

publisher = "Springer-Verlag Wien",

number = "1-2",

}

TY - JOUR

T1 - Plant myosins

AU - Shimmen, T.

AU - Ridge, R. W.

AU - Lambiris, I.

AU - Plazinski, J.

AU - Yokota, E.

AU - Williamson, R. E.

PY - 2000

Y1 - 2000

N2 - Plant myosins are motor proteins that bind to the external surfaces of organelles and interact with the cytoskeletal protein actin (as actin microfilaments), which organizes and directs intracellular movement. Recent progress in physiological, biochemical, immunological, and genetical studies of plant myosin has revealed considerable information about the structures and functions of these important molecules. This article briefly reviews the history of plant myosin research, summarizes recent progress, and highlights directions for future research.

AB - Plant myosins are motor proteins that bind to the external surfaces of organelles and interact with the cytoskeletal protein actin (as actin microfilaments), which organizes and directs intracellular movement. Recent progress in physiological, biochemical, immunological, and genetical studies of plant myosin has revealed considerable information about the structures and functions of these important molecules. This article briefly reviews the history of plant myosin research, summarizes recent progress, and highlights directions for future research.

KW - Actin filament

KW - Ca

KW - Calmodulin

KW - Cytoplasmic streaming

KW - Myosin

KW - Phosphorylation

UR - http://www.scopus.com/inward/record.url?scp=0033679546&partnerID=8YFLogxK

U2 - 10.1007/BF02524256

DO - 10.1007/BF02524256

M3 - Review article

SN - 0033-183X

VL - 214

SP - 1

EP - 10

JO - Protoplasma

JF - Protoplasma

IS - 1-2

ER -

Plant myosins

Abstract

Access to Document

Other files and links

Fingerprint

Cite this