ER sheet persistence is coupled to myosin 1c-regulated dynamic actin filament arrays.

Merja Susanna Joensuu, Ilya Belevich, Olli Rämö, Ilya Nevzorov, Helena Vihinen, Maija Kaarina Puhka, Tomasz Witkos, Martin Lowe, Maria Vartiainen, Eija Jokitalo

Research output: Contribution to journalArticleScientificpeer-review

Abstract

The endoplasmic reticulum (ER) comprises a dynamic three-dimensional (3D) network with diverse structural and functional domains. Proper ER operation requires an intricate balance within and between dynamics, morphology, and functions, but how these processes are coupled in cells has been unclear. Using live-cell imaging and 3D electron microscopy, we identify a specific subset of actin filaments localizing to polygons defined by ER sheets and tubules and describe a role for these actin arrays in ER sheet persistence and, thereby, in maintenance of the characteristic network architecture by showing that actin depolymerization leads to increased sheet fluctuation and transformations and results in small and less abundant sheet remnants and a defective ER network distribution. Furthermore, we identify myosin 1c localizing to the ER-associated actin filament arrays and reveal a novel role for myosin 1c in regulating these actin structures, as myosin 1c manipulations lead to loss of the actin filaments and to similar ER phenotype as observed after actin depolymerization. We propose that ER-associated actin filaments have a role in ER sheet persistence regulation and thus support the maintenance of sheets as a stationary subdomain of the dynamic ER network.
Original languageEnglish
JournalMolecular Biology of the Cell
Volume25
Issue number7
Pages (from-to)1111-26
Number of pages16
ISSN1059-1524
DOIs
Publication statusPublished - 1 Apr 2014
MoE publication typeA1 Journal article-refereed

Fields of Science

  • 1182 Biochemistry, cell and molecular biology

Cite this

@article{d69ebb533c9540ceb240e1f80dc0ff22,
title = "ER sheet persistence is coupled to myosin 1c-regulated dynamic actin filament arrays.",
abstract = "The endoplasmic reticulum (ER) comprises a dynamic three-dimensional (3D) network with diverse structural and functional domains. Proper ER operation requires an intricate balance within and between dynamics, morphology, and functions, but how these processes are coupled in cells has been unclear. Using live-cell imaging and 3D electron microscopy, we identify a specific subset of actin filaments localizing to polygons defined by ER sheets and tubules and describe a role for these actin arrays in ER sheet persistence and, thereby, in maintenance of the characteristic network architecture by showing that actin depolymerization leads to increased sheet fluctuation and transformations and results in small and less abundant sheet remnants and a defective ER network distribution. Furthermore, we identify myosin 1c localizing to the ER-associated actin filament arrays and reveal a novel role for myosin 1c in regulating these actin structures, as myosin 1c manipulations lead to loss of the actin filaments and to similar ER phenotype as observed after actin depolymerization. We propose that ER-associated actin filaments have a role in ER sheet persistence regulation and thus support the maintenance of sheets as a stationary subdomain of the dynamic ER network.",
keywords = "1182 Biochemistry, cell and molecular biology",
author = "Joensuu, {Merja Susanna} and Ilya Belevich and Olli R{\"a}m{\"o} and Ilya Nevzorov and Helena Vihinen and Puhka, {Maija Kaarina} and Tomasz Witkos and Martin Lowe and Maria Vartiainen and Eija Jokitalo",
year = "2014",
month = "4",
day = "1",
doi = "10.1091/mbc.E13-12-0712",
language = "English",
volume = "25",
pages = "1111--26",
journal = "Molecular Biology of the Cell",
issn = "1059-1524",
publisher = "AMERICAN SOCIETY FOR CELL BIOLOGY",
number = "7",

}

ER sheet persistence is coupled to myosin 1c-regulated dynamic actin filament arrays. / Joensuu, Merja Susanna; Belevich, Ilya; Rämö, Olli; Nevzorov, Ilya; Vihinen, Helena; Puhka, Maija Kaarina; Witkos, Tomasz; Lowe, Martin; Vartiainen, Maria; Jokitalo, Eija.

In: Molecular Biology of the Cell, Vol. 25, No. 7, 01.04.2014, p. 1111-26.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - ER sheet persistence is coupled to myosin 1c-regulated dynamic actin filament arrays.

AU - Joensuu, Merja Susanna

AU - Belevich, Ilya

AU - Rämö, Olli

AU - Nevzorov, Ilya

AU - Vihinen, Helena

AU - Puhka, Maija Kaarina

AU - Witkos, Tomasz

AU - Lowe, Martin

AU - Vartiainen, Maria

AU - Jokitalo, Eija

PY - 2014/4/1

Y1 - 2014/4/1

N2 - The endoplasmic reticulum (ER) comprises a dynamic three-dimensional (3D) network with diverse structural and functional domains. Proper ER operation requires an intricate balance within and between dynamics, morphology, and functions, but how these processes are coupled in cells has been unclear. Using live-cell imaging and 3D electron microscopy, we identify a specific subset of actin filaments localizing to polygons defined by ER sheets and tubules and describe a role for these actin arrays in ER sheet persistence and, thereby, in maintenance of the characteristic network architecture by showing that actin depolymerization leads to increased sheet fluctuation and transformations and results in small and less abundant sheet remnants and a defective ER network distribution. Furthermore, we identify myosin 1c localizing to the ER-associated actin filament arrays and reveal a novel role for myosin 1c in regulating these actin structures, as myosin 1c manipulations lead to loss of the actin filaments and to similar ER phenotype as observed after actin depolymerization. We propose that ER-associated actin filaments have a role in ER sheet persistence regulation and thus support the maintenance of sheets as a stationary subdomain of the dynamic ER network.

AB - The endoplasmic reticulum (ER) comprises a dynamic three-dimensional (3D) network with diverse structural and functional domains. Proper ER operation requires an intricate balance within and between dynamics, morphology, and functions, but how these processes are coupled in cells has been unclear. Using live-cell imaging and 3D electron microscopy, we identify a specific subset of actin filaments localizing to polygons defined by ER sheets and tubules and describe a role for these actin arrays in ER sheet persistence and, thereby, in maintenance of the characteristic network architecture by showing that actin depolymerization leads to increased sheet fluctuation and transformations and results in small and less abundant sheet remnants and a defective ER network distribution. Furthermore, we identify myosin 1c localizing to the ER-associated actin filament arrays and reveal a novel role for myosin 1c in regulating these actin structures, as myosin 1c manipulations lead to loss of the actin filaments and to similar ER phenotype as observed after actin depolymerization. We propose that ER-associated actin filaments have a role in ER sheet persistence regulation and thus support the maintenance of sheets as a stationary subdomain of the dynamic ER network.

KW - 1182 Biochemistry, cell and molecular biology

U2 - 10.1091/mbc.E13-12-0712

DO - 10.1091/mbc.E13-12-0712

M3 - Article

VL - 25

SP - 1111

EP - 1126

JO - Molecular Biology of the Cell

JF - Molecular Biology of the Cell

SN - 1059-1524

IS - 7

ER -