Highly multiplexed imaging uncovers changes in compositional noise within assembling focal adhesions

Integrin adhesome proteins bind each other in alternative manners, forming within the cell diverse cell-matrix adhesion sites with distinct properties. An intriguing question is how such modular assembly of adhesion sites is achieved correctly solely by self-organization of their components. Here we...

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Autores principales:	Harizanova, J., Fermin, Y., Malik-Sheriff, R.S., Wieczorek, J., Ickstadt, K., Grecco, H.E., Zamir, E.
Formato:	JOUR
Materias:	amino acid immunoglobulin G immunoglobulin M integrin paxillin zyxin bacterial protein cytoskeleton protein photoprotein tyrosine yellow fluorescent protein, Bacteria ZYX protein, human Article artificial neural network extracellular matrix feedback system focal adhesion image analysis markov chain mass spectrometry noise reduction protein analysis protein phosphorylation reproducibility fluorescence microscopy human image processing metabolism phosphorylation physiology procedures signal noise ratio signal processing Bacterial Proteins Cell-Matrix Junctions Cytoskeletal Proteins Focal Adhesions Humans Image Processing, Computer-Assisted Integrins Luminescent Proteins Microscopy, Fluorescence Paxillin Phosphorylation Signal Processing, Computer-Assisted Signal-To-Noise Ratio Tyrosine Zyxin
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_19326203_v11_n8_p_Harizanova
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_19326203_v11_n8_p_Harizanova
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spelling	todo:paper_19326203_v11_n8_p_Harizanova2023-10-03T16:34:44Z Highly multiplexed imaging uncovers changes in compositional noise within assembling focal adhesions Harizanova, J. Fermin, Y. Malik-Sheriff, R.S. Wieczorek, J. Ickstadt, K. Grecco, H.E. Zamir, E. amino acid immunoglobulin G immunoglobulin M integrin paxillin zyxin bacterial protein cytoskeleton protein integrin paxillin photoprotein tyrosine yellow fluorescent protein, Bacteria ZYX protein, human zyxin Article artificial neural network extracellular matrix feedback system focal adhesion image analysis markov chain mass spectrometry noise reduction protein analysis protein phosphorylation reproducibility fluorescence microscopy focal adhesion human image processing metabolism phosphorylation physiology procedures signal noise ratio signal processing Bacterial Proteins Cell-Matrix Junctions Cytoskeletal Proteins Focal Adhesions Humans Image Processing, Computer-Assisted Integrins Luminescent Proteins Microscopy, Fluorescence Paxillin Phosphorylation Signal Processing, Computer-Assisted Signal-To-Noise Ratio Tyrosine Zyxin Integrin adhesome proteins bind each other in alternative manners, forming within the cell diverse cell-matrix adhesion sites with distinct properties. An intriguing question is how such modular assembly of adhesion sites is achieved correctly solely by self-organization of their components. Here we address this question using high-throughput multiplexed imaging of eight proteins and two phosphorylation sites in a large number of single focal adhesions.We found that during the assembly of focal adhesions the variances of protein densities decrease while the correlations between them increase, suggesting reduction in the noise levels within these structures. These changes correlate independently with the area and internal density of focal adhesions, but not with their age or shape. Artificial neural network analysis indicates that a joint consideration of multiple components improves the predictability of paxillin and zyxin levels in internally dense focal adhesions. This suggests that paxillin and zyxin densities in focal adhesions are fine-tuned by integrating the levels of multiple other components, thus averaging-out stochastic fluctuations. Based on these results we propose that increase in internal protein densities facilitates noise suppression in focal adhesions, while noise suppression enables their stable growth and further density increase - hence forming a feedback loop giving rise to a quality-controlled assembly. © 2016 Harizanova et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Fil:Grecco, H.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_19326203_v11_n8_p_Harizanova
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	amino acid immunoglobulin G immunoglobulin M integrin paxillin zyxin bacterial protein cytoskeleton protein integrin paxillin photoprotein tyrosine yellow fluorescent protein, Bacteria ZYX protein, human zyxin Article artificial neural network extracellular matrix feedback system focal adhesion image analysis markov chain mass spectrometry noise reduction protein analysis protein phosphorylation reproducibility fluorescence microscopy focal adhesion human image processing metabolism phosphorylation physiology procedures signal noise ratio signal processing Bacterial Proteins Cell-Matrix Junctions Cytoskeletal Proteins Focal Adhesions Humans Image Processing, Computer-Assisted Integrins Luminescent Proteins Microscopy, Fluorescence Paxillin Phosphorylation Signal Processing, Computer-Assisted Signal-To-Noise Ratio Tyrosine Zyxin
spellingShingle	amino acid immunoglobulin G immunoglobulin M integrin paxillin zyxin bacterial protein cytoskeleton protein integrin paxillin photoprotein tyrosine yellow fluorescent protein, Bacteria ZYX protein, human zyxin Article artificial neural network extracellular matrix feedback system focal adhesion image analysis markov chain mass spectrometry noise reduction protein analysis protein phosphorylation reproducibility fluorescence microscopy focal adhesion human image processing metabolism phosphorylation physiology procedures signal noise ratio signal processing Bacterial Proteins Cell-Matrix Junctions Cytoskeletal Proteins Focal Adhesions Humans Image Processing, Computer-Assisted Integrins Luminescent Proteins Microscopy, Fluorescence Paxillin Phosphorylation Signal Processing, Computer-Assisted Signal-To-Noise Ratio Tyrosine Zyxin Harizanova, J. Fermin, Y. Malik-Sheriff, R.S. Wieczorek, J. Ickstadt, K. Grecco, H.E. Zamir, E. Highly multiplexed imaging uncovers changes in compositional noise within assembling focal adhesions
topic_facet	amino acid immunoglobulin G immunoglobulin M integrin paxillin zyxin bacterial protein cytoskeleton protein integrin paxillin photoprotein tyrosine yellow fluorescent protein, Bacteria ZYX protein, human zyxin Article artificial neural network extracellular matrix feedback system focal adhesion image analysis markov chain mass spectrometry noise reduction protein analysis protein phosphorylation reproducibility fluorescence microscopy focal adhesion human image processing metabolism phosphorylation physiology procedures signal noise ratio signal processing Bacterial Proteins Cell-Matrix Junctions Cytoskeletal Proteins Focal Adhesions Humans Image Processing, Computer-Assisted Integrins Luminescent Proteins Microscopy, Fluorescence Paxillin Phosphorylation Signal Processing, Computer-Assisted Signal-To-Noise Ratio Tyrosine Zyxin
description	Integrin adhesome proteins bind each other in alternative manners, forming within the cell diverse cell-matrix adhesion sites with distinct properties. An intriguing question is how such modular assembly of adhesion sites is achieved correctly solely by self-organization of their components. Here we address this question using high-throughput multiplexed imaging of eight proteins and two phosphorylation sites in a large number of single focal adhesions.We found that during the assembly of focal adhesions the variances of protein densities decrease while the correlations between them increase, suggesting reduction in the noise levels within these structures. These changes correlate independently with the area and internal density of focal adhesions, but not with their age or shape. Artificial neural network analysis indicates that a joint consideration of multiple components improves the predictability of paxillin and zyxin levels in internally dense focal adhesions. This suggests that paxillin and zyxin densities in focal adhesions are fine-tuned by integrating the levels of multiple other components, thus averaging-out stochastic fluctuations. Based on these results we propose that increase in internal protein densities facilitates noise suppression in focal adhesions, while noise suppression enables their stable growth and further density increase - hence forming a feedback loop giving rise to a quality-controlled assembly. © 2016 Harizanova et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
format	JOUR
author	Harizanova, J. Fermin, Y. Malik-Sheriff, R.S. Wieczorek, J. Ickstadt, K. Grecco, H.E. Zamir, E.
author_facet	Harizanova, J. Fermin, Y. Malik-Sheriff, R.S. Wieczorek, J. Ickstadt, K. Grecco, H.E. Zamir, E.
author_sort	Harizanova, J.
title	Highly multiplexed imaging uncovers changes in compositional noise within assembling focal adhesions
title_short	Highly multiplexed imaging uncovers changes in compositional noise within assembling focal adhesions
title_full	Highly multiplexed imaging uncovers changes in compositional noise within assembling focal adhesions
title_fullStr	Highly multiplexed imaging uncovers changes in compositional noise within assembling focal adhesions
title_full_unstemmed	Highly multiplexed imaging uncovers changes in compositional noise within assembling focal adhesions
title_sort	highly multiplexed imaging uncovers changes in compositional noise within assembling focal adhesions
url	http://hdl.handle.net/20.500.12110/paper_19326203_v11_n8_p_Harizanova
work_keys_str_mv	AT harizanovaj highlymultiplexedimaginguncoverschangesincompositionalnoisewithinassemblingfocaladhesions AT ferminy highlymultiplexedimaginguncoverschangesincompositionalnoisewithinassemblingfocaladhesions AT maliksheriffrs highlymultiplexedimaginguncoverschangesincompositionalnoisewithinassemblingfocaladhesions AT wieczorekj highlymultiplexedimaginguncoverschangesincompositionalnoisewithinassemblingfocaladhesions AT ickstadtk highlymultiplexedimaginguncoverschangesincompositionalnoisewithinassemblingfocaladhesions AT greccohe highlymultiplexedimaginguncoverschangesincompositionalnoisewithinassemblingfocaladhesions AT zamire highlymultiplexedimaginguncoverschangesincompositionalnoisewithinassemblingfocaladhesions
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Highly multiplexed imaging uncovers changes in compositional noise within assembling focal adhesions

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