Asset Details
Do you wish to reserve the book?
Sizes of actin networks sharing a common environment are determined by the relative rates of assembly
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Sizes of actin networks sharing a common environment are determined by the relative rates of assembly
Do you wish to request the book?
Sizes of actin networks sharing a common environment are determined by the relative rates of assembly
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Sizes of actin networks sharing a common environment are determined by the relative rates of assembly
2019
Overview
Within the cytoplasm of a single cell, several actin networks can coexist with distinct sizes, geometries, and protein compositions. These actin networks assemble in competition for a limited pool of proteins present in a common cellular environment. To predict how two distinct networks of actin filaments control this balance, the simultaneous assembly of actin-related protein 2/3 (Arp2/3)-branched networks and formin-linear networks of actin filaments around polystyrene microbeads was investigated with a range of actin accessory proteins (profilin, capping protein, actin-depolymerizing factor [ADF]/cofilin, and tropomyosin). Accessory proteins generally affected actin assembly rates for the distinct networks differently. These effects at the scale of individual actin networks were surprisingly not always correlated with corresponding loss-of-function phenotypes in cells. However, our observations agreed with a global interpretation, which compared relative actin assembly rates of individual actin networks. This work supports a general model in which the size of distinct actin networks is determined by their relative capacity to assemble in a common and competing environment.
Publisher
HAL CCSD,Public Library of Science,Public Library of Science (PLoS)
Subject
/ Actin Cytoskeleton - metabolism
/ Actin Depolymerizing Factors - metabolism
/ Actin-depolymerizing protein
/ Actin-Related Protein 2-3 Complex - metabolism
/ Actin-Related Protein 2-3 Complex - physiology
/ Animals
/ Assembly
/ Biochemistry, Molecular Biology
/ Cofilin
/ Humans
/ Insects
/ Kinetics
/ Microfilament Proteins - metabolism
/ Microfilament Proteins - physiology
/ Motility
/ Profilin
/ Protein Interaction Maps - physiology
/ Proteins
/ Research and Analysis Methods
/ Yeast
