Plasmodesmata viewed as specialised membrane adhesion sites

Jens Tilsner; Khalid Amari; Lesley Torrance

doi:10.1007/s00709-010-0217-6

Plasmodesmata viewed as specialised membrane adhesion sites

Jens Tilsner, Khalid Amari, Lesley Torrance

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

Abstract

A significant amount of work has been expended to identify the elusive components of plasmodesmata (PD) to help understand their structure, as well as how proteins are targeted to them. This review focuses on the role that lipid membranes may play in defining PD both structurally and as subcellular targeting addresses. Parallels are drawn to findings in other areas of research which focus on the lateral segregation of membrane domains and the generation of three-dimensional organellar shapes from flat lipid bilayers. We conclude that consideration of the protein-lipid interactions in cell biological studies of PD components and PD-targeted proteins may yield new insights into some of the many open questions regarding these unique structures.

Original language	English
Pages (from-to)	39-60
Number of pages	22
Journal	Protoplasma
Volume	248
Issue number	1
DOIs	https://doi.org/10.1007/s00709-010-0217-6
Publication status	Published - Jan 2011

Keywords

Plasmodesma
Protein-lipid interaction
Lipid rafts
Membrane curvature
Endomembranes
Subcellular targeting
TOBACCO-MOSAIC-VIRUS
CELL-TO-CELL
VIRAL MOVEMENT PROTEINS
TRIPLE GENE BLOCK
CORTICAL ENDOPLASMIC-RETICULUM
MAIZE MESOCOTYL PLASMODESMATA
DETERGENT-RESISTANT MEMBRANES
SIZE-EXCLUSION LIMIT
GLOBULAR TAIL DOMAIN
MYOSIN-LIKE PROTEIN

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10.1007/s00709-010-0217-6

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title = "Plasmodesmata viewed as specialised membrane adhesion sites",

abstract = "A significant amount of work has been expended to identify the elusive components of plasmodesmata (PD) to help understand their structure, as well as how proteins are targeted to them. This review focuses on the role that lipid membranes may play in defining PD both structurally and as subcellular targeting addresses. Parallels are drawn to findings in other areas of research which focus on the lateral segregation of membrane domains and the generation of three-dimensional organellar shapes from flat lipid bilayers. We conclude that consideration of the protein-lipid interactions in cell biological studies of PD components and PD-targeted proteins may yield new insights into some of the many open questions regarding these unique structures.",

keywords = "Plasmodesma, Protein-lipid interaction, Lipid rafts, Membrane curvature, Endomembranes, Subcellular targeting, TOBACCO-MOSAIC-VIRUS, CELL-TO-CELL, VIRAL MOVEMENT PROTEINS, TRIPLE GENE BLOCK, CORTICAL ENDOPLASMIC-RETICULUM, MAIZE MESOCOTYL PLASMODESMATA, DETERGENT-RESISTANT MEMBRANES, SIZE-EXCLUSION LIMIT, GLOBULAR TAIL DOMAIN, MYOSIN-LIKE PROTEIN",

author = "Jens Tilsner and Khalid Amari and Lesley Torrance",

year = "2011",

month = jan,

doi = "10.1007/s00709-010-0217-6",

language = "English",

volume = "248",

pages = "39--60",

journal = "Protoplasma",

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publisher = "Springer",

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T1 - Plasmodesmata viewed as specialised membrane adhesion sites

AU - Tilsner, Jens

AU - Amari, Khalid

AU - Torrance, Lesley

PY - 2011/1

Y1 - 2011/1

N2 - A significant amount of work has been expended to identify the elusive components of plasmodesmata (PD) to help understand their structure, as well as how proteins are targeted to them. This review focuses on the role that lipid membranes may play in defining PD both structurally and as subcellular targeting addresses. Parallels are drawn to findings in other areas of research which focus on the lateral segregation of membrane domains and the generation of three-dimensional organellar shapes from flat lipid bilayers. We conclude that consideration of the protein-lipid interactions in cell biological studies of PD components and PD-targeted proteins may yield new insights into some of the many open questions regarding these unique structures.

AB - A significant amount of work has been expended to identify the elusive components of plasmodesmata (PD) to help understand their structure, as well as how proteins are targeted to them. This review focuses on the role that lipid membranes may play in defining PD both structurally and as subcellular targeting addresses. Parallels are drawn to findings in other areas of research which focus on the lateral segregation of membrane domains and the generation of three-dimensional organellar shapes from flat lipid bilayers. We conclude that consideration of the protein-lipid interactions in cell biological studies of PD components and PD-targeted proteins may yield new insights into some of the many open questions regarding these unique structures.

KW - Plasmodesma

KW - Protein-lipid interaction

KW - Lipid rafts

KW - Membrane curvature

KW - Endomembranes

KW - Subcellular targeting

KW - TOBACCO-MOSAIC-VIRUS

KW - CELL-TO-CELL

KW - VIRAL MOVEMENT PROTEINS

KW - TRIPLE GENE BLOCK

KW - CORTICAL ENDOPLASMIC-RETICULUM

KW - MAIZE MESOCOTYL PLASMODESMATA

KW - DETERGENT-RESISTANT MEMBRANES

KW - SIZE-EXCLUSION LIMIT

KW - GLOBULAR TAIL DOMAIN

KW - MYOSIN-LIKE PROTEIN

U2 - 10.1007/s00709-010-0217-6

DO - 10.1007/s00709-010-0217-6

M3 - Review article

SN - 0033-183X

VL - 248

SP - 39

EP - 60

JO - Protoplasma

JF - Protoplasma

IS - 1

ER -

Plasmodesmata viewed as specialised membrane adhesion sites

Abstract

Keywords

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