The ERC1 scaffold protein implicated in cell motility drives the assembly of a liquid phase

Kristyna Sala, Agnese Corbetta, Claudia Minici, Diletta Tonoli, David H. Murray, Eugenia Cammarota, Lucrezia Ribolla, Martina Ramella, Riccardo Fesce, Davide Mazza, Massimo Degano, Ivan de Curtis

Research output: Contribution to journalArticle

26 Downloads (Pure)

Abstract

Several cellular processes depend on networks of proteins assembled at specific sites near the plasma membrane. Scaffold proteins assemble these networks by recruiting relevant molecules. The scaffold protein ERC1/ELKS and its partners promote cell migration and invasion, and assemble into dynamic networks at the protruding edge of cells. Here by electron microscopy and single molecule analysis we identify ERC1 as an extended flexible dimer. We found that ERC1 scaffolds form cytoplasmic condensates with a behavior that is consistent with liquid phases that are modulated by a predicted disordered region of ERC1. These condensates specifically host partners of a network relevant to cell motility, including liprin-α1, which was unnecessary for the formation of condensates, but influenced their dynamic behavior. Phase separation at specific sites of the cell periphery may represent an elegant mechanism to control the assembly and turnover of dynamic scaffolds needed for the spatial localization and processing of molecules.

Original languageEnglish
Article number13530
Pages (from-to)1-14
Number of pages14
JournalScientific Reports
Volume9
DOIs
Publication statusPublished - 19 Sep 2019

Fingerprint

Cell Movement
Proteins
Electron Microscopy
Cell Membrane
Drive
Spatial Processing

Cite this

Sala, K., Corbetta, A., Minici, C., Tonoli, D., Murray, D. H., Cammarota, E., ... de Curtis, I. (2019). The ERC1 scaffold protein implicated in cell motility drives the assembly of a liquid phase. Scientific Reports, 9, 1-14. [13530]. https://doi.org/10.1038/s41598-019-49630-y
Sala, Kristyna ; Corbetta, Agnese ; Minici, Claudia ; Tonoli, Diletta ; Murray, David H. ; Cammarota, Eugenia ; Ribolla, Lucrezia ; Ramella, Martina ; Fesce, Riccardo ; Mazza, Davide ; Degano, Massimo ; de Curtis, Ivan. / The ERC1 scaffold protein implicated in cell motility drives the assembly of a liquid phase. In: Scientific Reports. 2019 ; Vol. 9. pp. 1-14.
@article{8402029608d74fe78e0dd29815e33e78,
title = "The ERC1 scaffold protein implicated in cell motility drives the assembly of a liquid phase",
abstract = "Several cellular processes depend on networks of proteins assembled at specific sites near the plasma membrane. Scaffold proteins assemble these networks by recruiting relevant molecules. The scaffold protein ERC1/ELKS and its partners promote cell migration and invasion, and assemble into dynamic networks at the protruding edge of cells. Here by electron microscopy and single molecule analysis we identify ERC1 as an extended flexible dimer. We found that ERC1 scaffolds form cytoplasmic condensates with a behavior that is consistent with liquid phases that are modulated by a predicted disordered region of ERC1. These condensates specifically host partners of a network relevant to cell motility, including liprin-α1, which was unnecessary for the formation of condensates, but influenced their dynamic behavior. Phase separation at specific sites of the cell periphery may represent an elegant mechanism to control the assembly and turnover of dynamic scaffolds needed for the spatial localization and processing of molecules.",
author = "Kristyna Sala and Agnese Corbetta and Claudia Minici and Diletta Tonoli and Murray, {David H.} and Eugenia Cammarota and Lucrezia Ribolla and Martina Ramella and Riccardo Fesce and Davide Mazza and Massimo Degano and {de Curtis}, Ivan",
year = "2019",
month = "9",
day = "19",
doi = "10.1038/s41598-019-49630-y",
language = "English",
volume = "9",
pages = "1--14",
journal = "Scientific Reports",
issn = "2045-2322",
publisher = "Nature Publishing Group",

}

Sala, K, Corbetta, A, Minici, C, Tonoli, D, Murray, DH, Cammarota, E, Ribolla, L, Ramella, M, Fesce, R, Mazza, D, Degano, M & de Curtis, I 2019, 'The ERC1 scaffold protein implicated in cell motility drives the assembly of a liquid phase', Scientific Reports, vol. 9, 13530, pp. 1-14. https://doi.org/10.1038/s41598-019-49630-y

The ERC1 scaffold protein implicated in cell motility drives the assembly of a liquid phase. / Sala, Kristyna; Corbetta, Agnese; Minici, Claudia; Tonoli, Diletta; Murray, David H.; Cammarota, Eugenia; Ribolla, Lucrezia; Ramella, Martina; Fesce, Riccardo; Mazza, Davide; Degano, Massimo; de Curtis, Ivan.

In: Scientific Reports, Vol. 9, 13530, 19.09.2019, p. 1-14.

Research output: Contribution to journalArticle

TY - JOUR

T1 - The ERC1 scaffold protein implicated in cell motility drives the assembly of a liquid phase

AU - Sala, Kristyna

AU - Corbetta, Agnese

AU - Minici, Claudia

AU - Tonoli, Diletta

AU - Murray, David H.

AU - Cammarota, Eugenia

AU - Ribolla, Lucrezia

AU - Ramella, Martina

AU - Fesce, Riccardo

AU - Mazza, Davide

AU - Degano, Massimo

AU - de Curtis, Ivan

PY - 2019/9/19

Y1 - 2019/9/19

N2 - Several cellular processes depend on networks of proteins assembled at specific sites near the plasma membrane. Scaffold proteins assemble these networks by recruiting relevant molecules. The scaffold protein ERC1/ELKS and its partners promote cell migration and invasion, and assemble into dynamic networks at the protruding edge of cells. Here by electron microscopy and single molecule analysis we identify ERC1 as an extended flexible dimer. We found that ERC1 scaffolds form cytoplasmic condensates with a behavior that is consistent with liquid phases that are modulated by a predicted disordered region of ERC1. These condensates specifically host partners of a network relevant to cell motility, including liprin-α1, which was unnecessary for the formation of condensates, but influenced their dynamic behavior. Phase separation at specific sites of the cell periphery may represent an elegant mechanism to control the assembly and turnover of dynamic scaffolds needed for the spatial localization and processing of molecules.

AB - Several cellular processes depend on networks of proteins assembled at specific sites near the plasma membrane. Scaffold proteins assemble these networks by recruiting relevant molecules. The scaffold protein ERC1/ELKS and its partners promote cell migration and invasion, and assemble into dynamic networks at the protruding edge of cells. Here by electron microscopy and single molecule analysis we identify ERC1 as an extended flexible dimer. We found that ERC1 scaffolds form cytoplasmic condensates with a behavior that is consistent with liquid phases that are modulated by a predicted disordered region of ERC1. These condensates specifically host partners of a network relevant to cell motility, including liprin-α1, which was unnecessary for the formation of condensates, but influenced their dynamic behavior. Phase separation at specific sites of the cell periphery may represent an elegant mechanism to control the assembly and turnover of dynamic scaffolds needed for the spatial localization and processing of molecules.

UR - http://www.scopus.com/inward/record.url?scp=85072408207&partnerID=8YFLogxK

U2 - 10.1038/s41598-019-49630-y

DO - 10.1038/s41598-019-49630-y

M3 - Article

C2 - 31537859

VL - 9

SP - 1

EP - 14

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

M1 - 13530

ER -