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Article ; Online: Deadly actin collapse by disulfidptosis.

Machesky, Laura M

2023 Volume 25, Issue 3, Page(s) 375–376

MeSH term(s)	Actins ; Cytoskeleton
Chemical Substances	Actins
Language	English
Publishing date	2023-03-07
Publishing country	England
Document type	Journal Article ; Comment
ZDB-ID	1474722-4
ISSN	1476-4679 ; 1465-7392
ISSN (online)	1476-4679
ISSN	1465-7392
DOI	10.1038/s41556-023-01100-4
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Zs.A 5169: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 12: Show issues

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Article ; Online: CYRI proteins: controllers of actin dynamics in the cellular 'eat vs walk' decision.

Machesky, Laura M

Biochemical Society transactions

2023 Volume 51, Issue 2, Page(s) 579–585

Abstract: Cells use actin-based protrusions not only to migrate, but also to sample their environment and take up liquids and particles, including nutrients, antigens and pathogens. Lamellipodia are sheet-like actin-based protrusions involved in sensing the ... ...

Abstract	Cells use actin-based protrusions not only to migrate, but also to sample their environment and take up liquids and particles, including nutrients, antigens and pathogens. Lamellipodia are sheet-like actin-based protrusions involved in sensing the substratum and directing cell migration. Related structures, macropinocytic cups, arise from lamellipodia ruffles and can take in large gulps of the surrounding medium. How cells regulate the balance between using lamellipodia for migration and macropinocytosis is not yet well understood. We recently identified CYRI proteins as RAC1-binding regulators of the dynamics of lamellipodia and macropinocytic events. This review discusses recent advances in our understanding of how cells regulate the balance between eating and walking by repurposing their actin cytoskeletons in response to environmental cues.
MeSH term(s)	Actins/metabolism ; Cell Movement ; Actin Cytoskeleton/metabolism ; Cell Membrane Structures/metabolism ; Pseudopodia/metabolism ; Walking
Chemical Substances	Actins
Language	English
Publishing date	2023-01-03
Publishing country	England
Document type	Review ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	184237-7
ISSN	1470-8752 ; 0300-5127
ISSN (online)	1470-8752
ISSN	0300-5127
DOI	10.1042/BST20221354
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Zs.A 944: Show issues

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Article ; Online: Dichotomous role of the serine/threonine kinase MAP4K4 in pancreatic ductal adenocarcinoma onset and metastasis through control of AKT and ERK pathways.

Juin, Amelie / Spence, Heather J / Machesky, Laura M

The Journal of pathology

2024 Volume 262, Issue 4, Page(s) 454–466

Abstract: MAP4K4 is a serine/threonine kinase of the STE20 family involved in the regulation of actin cytoskeleton dynamics and cell motility. It has been proposed as a target of angiogenesis and inhibitors show potential in cardioprotection. MAP4K4 also mediates ... ...

Abstract	MAP4K4 is a serine/threonine kinase of the STE20 family involved in the regulation of actin cytoskeleton dynamics and cell motility. It has been proposed as a target of angiogenesis and inhibitors show potential in cardioprotection. MAP4K4 also mediates cell invasion in vitro, is overexpressed in various types of cancer, and is associated with poor patient prognosis. Recently, MAP4K4 has been shown to be overexpressed in pancreatic cancer, but its role in tumour initiation, progression, and metastasis is unknown. Here, using the Kras
MeSH term(s)	Animals ; Mice ; Humans ; Proto-Oncogene Proteins c-akt/metabolism ; Proto-Oncogene Proteins p21(ras)/genetics ; Proto-Oncogene Proteins p21(ras)/metabolism ; MAP Kinase Signaling System ; Cell Line, Tumor ; Pancreatic Neoplasms/pathology ; Carcinoma, Pancreatic Ductal/pathology ; Protein Serine-Threonine Kinases/genetics ; Protein Serine-Threonine Kinases/metabolism ; Serine ; Intracellular Signaling Peptides and Proteins/metabolism
Chemical Substances	Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; Proto-Oncogene Proteins p21(ras) (EC 3.6.5.2) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; Serine (452VLY9402) ; MAP4K4 protein, human (EC 2.7.1.11) ; Intracellular Signaling Peptides and Proteins
Language	English
Publishing date	2024-01-17
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3119-7
ISSN	1096-9896 ; 0022-3417
ISSN (online)	1096-9896
ISSN	0022-3417
DOI	10.1002/path.6248
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Ud II Zs.12: Show issues

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Article ; Online: Image-based Quantification of Macropinocytosis Using Dextran Uptake into Cultured Cells.

Le, Anh H / Machesky, Laura M

Bio-protocol

2022 Volume 12, Issue 7, Page(s) e4367

Abstract: Macropinocytosis is an evolutionarily conserved process, which is characterized by the formation of membrane ruffles and the uptake of extracellular fluid. We recently demonstrated a role for CYFIP-related Rac1 Interactor (CYRI) proteins in ... ...

Abstract	Macropinocytosis is an evolutionarily conserved process, which is characterized by the formation of membrane ruffles and the uptake of extracellular fluid. We recently demonstrated a role for CYFIP-related Rac1 Interactor (CYRI) proteins in macropinocytosis. High-molecular weight dextran (70kDa or higher) has generally been used as a marker for macropinocytosis because it is too large to fit in smaller endocytic vesicles, such as those of clathrin or caveolin-mediated endocytosis. Through the use of an image-based dextran uptake assay, we showed that cells lacking CYRI proteins internalise less dextran compared to their wild-type counterparts. Here, we will describe a step-by-step experimentation procedure to detect internalised dextran in cultured cells, and an image pipeline to analyse the acquired images, using the open-access software ImageJ/Fiji. This protocol is detailed yet simple and easily adaptable to different treatment conditions, and the analysis can also be automated for improved processing speed.
Language	English
Publishing date	2022-04-05
Publishing country	United States
Document type	Journal Article
ZDB-ID	2833269-6
ISSN	2331-8325 ; 2331-8325
ISSN (online)	2331-8325
ISSN	2331-8325
DOI	10.21769/BioProtoc.4367
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Article ; Online: Rab11FIP proteins link endocytic recycling vesicles for cytoskeletal transport and tethering.

Machesky, Laura M

Bioscience reports

2019 Volume 39, Issue 1

Abstract: Regulated trafficking of internalised integrins and growth factor receptors enables polarisation of morphology and motility and enables lumen formation in multicellular structures. Recycling vesicles marked with Rab11 direct internalised cargo back to ... ...

Abstract	Regulated trafficking of internalised integrins and growth factor receptors enables polarisation of morphology and motility and enables lumen formation in multicellular structures. Recycling vesicles marked with Rab11 direct internalised cargo back to the plasma membrane to affect biological processes such as polarised trafficking and cancer cell invasion. A recent study by Ji and colleagues, provides insight into how the trafficking protein Rab11FIP2 links with the actin-based motor myo5b and the small GTPase Rab11 to regulate vesicle tethering and transport along actin filaments [1]. The authors used biochemical methods to demonstrate that Rab11a binds directly to the tail of myo5b and that Rab11FIP2 also forms direct interactions with both Rab11a and myo5b tails. These proteins essentially compete for binding to similar regions and thus can regulate the association and activity of each other. Ji and colleagues further demonstrate that Rab11a activates myo5b by binding to its globular tail and relieving a head-tail autoinhibition. Due to differing affinities between Rab11 and myo5b or Rab11FIP2, they propose that Rab11FIP2 mediates the association of myo5b with cargo vesicles, while Rab11a regulates the motor activity of myo5b. The present study thus elucidates how myo5b is regulated by its interactions with Rab11a and Rab11FIP2 and proposes a model for coordination of recycling vesicle tethering and motor activity. The present study has implications for how cells control polarity and motility in health and disease and suggests how Rab11FIP proteins might control motor protein activity and engagement for transport.
MeSH term(s)	Cell Membrane ; Membrane Proteins ; Myosins ; Protein Transport ; rab GTP-Binding Proteins
Chemical Substances	Membrane Proteins ; Myosins (EC 3.6.4.1) ; rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2019-01-30
Publishing country	England
Document type	Journal Article ; Comment
ZDB-ID	764946-0
ISSN	1573-4935 ; 0144-8463
ISSN (online)	1573-4935
ISSN	0144-8463
DOI	10.1042/BSR20182219
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Zs.A 1676: Show issues

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Article ; Online: WAVE complex regulation by force.

Machesky, Laura M / Insall, Robert H

Nature cell biology

2021 Volume 23, Issue 11, Page(s) 1111–1112

MeSH term(s)	Mechanical Phenomena
Language	English
Publishing date	2021-11-04
Publishing country	England
Document type	Journal Article ; Comment
ZDB-ID	1474722-4
ISSN	1476-4679 ; 1465-7392
ISSN (online)	1476-4679
ISSN	1465-7392
DOI	10.1038/s41556-021-00790-y
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Zs.A 5169: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 12: Show issues

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Article ; Online: MICAL2 fine-tunes Arp2/3 for actin branching.

Olson, Michael F / Machesky, Laura M

The Journal of cell biology

2021 Volume 220, Issue 8

Abstract: The ARP2/3 complex promotes branched actin networks, but the importance of specific subunit isoforms is unclear. In this issue, Galloni, Carra, et al. (2021. J. Cell Biol. https://doi.org/10.1083/jcb.202102043) show that MICAL2 mediates methionine ... ...

Abstract	The ARP2/3 complex promotes branched actin networks, but the importance of specific subunit isoforms is unclear. In this issue, Galloni, Carra, et al. (2021. J. Cell Biol. https://doi.org/10.1083/jcb.202102043) show that MICAL2 mediates methionine oxidation of ARP3B, thus destabilizing ARP2/3 complexes and leading to disassembly of branched actin filaments.
MeSH term(s)	Actin Cytoskeleton ; Actin-Related Protein 2-3 Complex/genetics ; Actins
Chemical Substances	Actin-Related Protein 2-3 Complex ; Actins
Language	English
Publishing date	2021-07-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Comment
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202106176
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Ub I Zs.190: Show issues

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Article ; Online: The liver metastatic niche: modelling the extracellular matrix in metastasis.

Drew, James / Machesky, Laura M

Disease models & mechanisms

2021 Volume 14, Issue 4

Abstract: Dissemination of malignant cells from primary tumours to metastatic sites is a key step in cancer progression. Disseminated tumour cells preferentially settle in specific target organs, and the success of such metastases depends on dynamic interactions ... ...

Abstract	Dissemination of malignant cells from primary tumours to metastatic sites is a key step in cancer progression. Disseminated tumour cells preferentially settle in specific target organs, and the success of such metastases depends on dynamic interactions between cancer cells and the microenvironments they encounter at secondary sites. Two emerging concepts concerning the biology of metastasis are that organ-specific microenvironments influence the fate of disseminated cancer cells, and that cancer cell-extracellular matrix interactions have important roles at all stages of the metastatic cascade. The extracellular matrix is the complex and dynamic non-cellular component of tissues that provides a physical scaffold and conveys essential adhesive and paracrine signals for a tissue's function. Here, we focus on how extracellular matrix dynamics contribute to liver metastases - a common and deadly event. We discuss how matrix components of the healthy and premetastatic liver support early seeding of disseminated cancer cells, and how the matrix derived from both cancer and liver contributes to the changes in niche composition as metastasis progresses. We also highlight the technical developments that are providing new insights into the stochastic, dynamic and multifaceted roles of the liver extracellular matrix in permitting and sustaining metastasis. An understanding of the contribution of the extracellular matrix to different stages of metastasis may well pave the way to targeted and effective therapies against metastatic disease.
MeSH term(s)	Animals ; Epithelial-Mesenchymal Transition ; Extracellular Matrix/metabolism ; Humans ; Liver Neoplasms/pathology ; Models, Biological ; Neoplasm Metastasis ; Neoplastic Cells, Circulating/pathology
Language	English
Publishing date	2021-04-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2451104-3
ISSN	1754-8411 ; 1754-8403
ISSN (online)	1754-8411
ISSN	1754-8403
DOI	10.1242/dmm.048801
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Article ; Online: FSCN1 and epithelial mesenchymal transformation transcription factor expression in human pancreatic intraepithelial neoplasia and ductal adenocarcinoma.

Morris, Hayley T / Bamlet, William R / Razidlo, Gina L / Machesky, Laura M

Pathology, research and practice

2023 Volume 251, Page(s) 154836

Abstract: Background: The actin regulatory protein fascin (FSCN1) and epithelial mesenchymal transition (EMT) transcription factor (TF) SLUG/SNAI2 have been shown to be expressed in PDAC and its precursor lesions (pancreatic intraepithelial neoplasia (PanIN), ... ...

Abstract	Background: The actin regulatory protein fascin (FSCN1) and epithelial mesenchymal transition (EMT) transcription factor (TF) SLUG/SNAI2 have been shown to be expressed in PDAC and its precursor lesions (pancreatic intraepithelial neoplasia (PanIN), graded 1-3) in in vitro and murine in vivo studies. Our aim was to investigate the expression of FSCN1 and EMT-TFs and their association with survival in human PanIN and PDAC. Methods: Expression was investigated in silico using TCGA PanCancer Atlas data (177 PDAC samples with mRNA data) and immunohistochemical staining of a tissue microarray (TMA) (59 PDAC patients). Results: High FSCN1 expression was associated with poorer overall survival (p = 0.02) in the TCGA data. EMT-TF expression was not associated with survival, however FSCN1 expression correlated with that of the EMT-TFs SLUG/SNAI2 (rho = 0.49, p < 0.001) and TWIST1 (rho = 0.52, p < 0.001). TMA IHC showed low expression of SNAI2 and TWIST1 in normal ductal epithelium, while FSCN1 was not expressed. SNAI2 increased slightly in PanIN1-2, then decreased in higher grade lesions. TWIST1 increased in PanIN2-3 and was retained in PDAC. FSCN1 was increasingly expressed from PanIN2 onwards. SNAI2 and TWIST1 expression positively correlated in all grades of PanIN and PDAC (rho = 0.52, p < 0.001). FSCN1 correlated positively with SNAI2 in PanIN1 (rho = 0.56, p < 0.01). Conclusions: Increased expression of EMT-TFs in low-grade PanIN followed by FSCN1 in PanIN3 and PDAC suggests EMT-TFs may trigger FSCN1 expression and are potential early diagnostic markers. FSCN1 expression correlated with overall survival in PDAC and may have value as a prognostic marker.
MeSH term(s)	Humans ; Carcinoma in Situ/pathology ; Carcinoma, Pancreatic Ductal/pathology ; Carrier Proteins ; Epithelial-Mesenchymal Transition/genetics ; Microfilament Proteins/metabolism ; Pancreatic Neoplasms/pathology ; Transcription Factors/metabolism
Chemical Substances	Carrier Proteins ; fascin (146808-54-0) ; FSCN1 protein, human ; Microfilament Proteins ; Transcription Factors ; SNAI2 protein, human
Language	English
Publishing date	2023-10-02
Publishing country	Germany
Document type	Journal Article
ZDB-ID	391889-0
ISSN	1618-0631 ; 0344-0338
ISSN (online)	1618-0631
ISSN	0344-0338
DOI	10.1016/j.prp.2023.154836
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Ud III Zs.20: Show issues

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Article ; Online: The cell pushes back: The Arp2/3 complex is a key orchestrator of cellular responses to environmental forces.

Papalazarou, Vassilis / Machesky, Laura M

Current opinion in cell biology

2020 Volume 68, Page(s) 37–44

Abstract: The Arp2/3 complex orchestrates the formation of branched actin networks at the interface between the cytoplasm and membranes. Although it is widely appreciated that these networks are useful for scaffolding, creating pushing forces and delineating zones ...

Abstract	The Arp2/3 complex orchestrates the formation of branched actin networks at the interface between the cytoplasm and membranes. Although it is widely appreciated that these networks are useful for scaffolding, creating pushing forces and delineating zones at the membrane interface, it has only recently come to light that branched actin networks are mechanosensitive, giving them special properties. Here, we discuss recent advances in our understanding of how Arp2/3-generated actin networks respond to load forces and thus allow cells to create pushing forces in responsive and tuneable ways to effect cellular processes such as migration, invasion, phagocytosis, adhesion and even nuclear and DNA damage repair.
MeSH term(s)	Actin Cytoskeleton/metabolism ; Actin-Related Protein 2-3 Complex/physiology ; Animals ; Cell Movement ; Cell Nucleus/metabolism ; Extracellular Matrix/metabolism ; Humans ; Intercellular Junctions ; Mechanotransduction, Cellular ; Yeasts
Chemical Substances	Actin-Related Protein 2-3 Complex
Language	English
Publishing date	2020-09-22
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1026381-0
ISSN	1879-0410 ; 0955-0674
ISSN (online)	1879-0410
ISSN	0955-0674
DOI	10.1016/j.ceb.2020.08.012
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