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Article: Ca

Enrich, Carlos / Lu, Albert / Tebar, Francesc / Rentero, Carles / Grewal, Thomas

Advances in experimental medicine and biology

2023 Volume 1422, Page(s) 393–438

Abstract: Maintaining lipid composition diversity in membranes from different organelles is critical for numerous cellular processes. However, many lipids are synthesized in the endoplasmic reticulum (ER) and require delivery to other organelles. In this scenario, ...

Abstract	Maintaining lipid composition diversity in membranes from different organelles is critical for numerous cellular processes. However, many lipids are synthesized in the endoplasmic reticulum (ER) and require delivery to other organelles. In this scenario, formation of membrane contact sites (MCS) between neighbouring organelles has emerged as a novel non-vesicular lipid transport mechanism. Dissecting the molecular composition of MCS identified phosphoinositides (PIs), cholesterol, scaffolding/tethering proteins as well as Ca
MeSH term(s)	Phosphatidylinositols/metabolism ; Annexins/metabolism ; Cell Membrane/metabolism ; Endoplasmic Reticulum/metabolism ; Carrier Proteins/metabolism ; Cholesterol/metabolism
Chemical Substances	Phosphatidylinositols ; Annexins ; Carrier Proteins ; Cholesterol (97C5T2UQ7J)
Language	English
Publishing date	2023-03-29
Publishing country	United States
Document type	Journal Article
ISSN	2214-8019 ; 0065-2598
ISSN (online)	2214-8019
ISSN	0065-2598
DOI	10.1007/978-3-031-21547-6_15
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Article: Annexins Bridging the Gap: Novel Roles in Membrane Contact Site Formation.

Enrich, Carlos / Lu, Albert / Tebar, Francesc / Rentero, Carles / Grewal, Thomas

Frontiers in cell and developmental biology

2022 Volume 9, Page(s) 797949

Abstract: Membrane contact sites (MCS) are specialized small areas of close apposition between two different organelles that have led researchers to reconsider the dogma of intercellular ... ...

Abstract	Membrane contact sites (MCS) are specialized small areas of close apposition between two different organelles that have led researchers to reconsider the dogma of intercellular communication
Language	English
Publishing date	2022-01-06
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2737824-X
ISSN	2296-634X
ISSN	2296-634X
DOI	10.3389/fcell.2021.797949
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Article: GTPases Rac1 and Ras Signaling from Endosomes.

Tebar, Francesc / Enrich, Carlos / Rentero, Carles / Grewal, Thomas

Progress in molecular and subcellular biology

2018 Volume 57, Page(s) 65–105

Abstract: The endocytic compartment is not only the functional continuity of the plasma membrane but consists of a diverse collection of intracellular heterogeneous complex structures that transport, amplify, sustain, and/or sort signaling molecules. Over the ... ...

Abstract	The endocytic compartment is not only the functional continuity of the plasma membrane but consists of a diverse collection of intracellular heterogeneous complex structures that transport, amplify, sustain, and/or sort signaling molecules. Over the years, it has become evident that early, late, and recycling endosomes represent an interconnected vesicular-tubular network able to form signaling platforms that dynamically and efficiently translate extracellular signals into biological outcome. Cell activation, differentiation, migration, death, and survival are some of the endpoints of endosomal signaling. Hence, to understand the role of the endosomal system in signal transduction in space and time, it is therefore necessary to dissect and identify the plethora of decoders that are operational in the different steps along the endocytic pathway. In this chapter, we focus on the regulation of spatiotemporal signaling in cells, considering endosomes as central platforms, in which several small GTPases proteins of the Ras superfamily, in particular Ras and Rac1, actively participate to control cellular processes like proliferation and cell mobility.
MeSH term(s)	Cell Movement/genetics ; Cell Proliferation/genetics ; Endocytosis/genetics ; Endosomes/genetics ; Humans ; Protein Transport ; Signal Transduction/genetics ; rac1 GTP-Binding Protein/genetics ; ras Proteins/genetics
Chemical Substances	rac1 GTP-Binding Protein (EC 3.6.5.2) ; ras Proteins (EC 3.6.5.2)
Language	English
Publishing date	2018-08-10
Publishing country	United States
Document type	Journal Article ; Review
ISSN	0079-6484
ISSN	0079-6484
DOI	10.1007/978-3-319-96704-2_3
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Article ; Online: Pleiotropic Roles of Calmodulin in the Regulation of KRas and Rac1 GTPases: Functional Diversity in Health and Disease.

Tebar, Francesc / Chavero, Albert / Agell, Neus / Lu, Albert / Rentero, Carles / Enrich, Carlos / Grewal, Thomas

International journal of molecular sciences

2020 Volume 21, Issue 10

Abstract: Calmodulin is a ubiquitous signalling protein that controls many biological processes due to its capacity to interact and/or regulate a large number of cellular proteins and pathways, mostly in a ... ...

Abstract	Calmodulin is a ubiquitous signalling protein that controls many biological processes due to its capacity to interact and/or regulate a large number of cellular proteins and pathways, mostly in a Ca
MeSH term(s)	Animals ; Calmodulin/genetics ; Calmodulin/metabolism ; Carcinogenesis/genetics ; Carcinogenesis/metabolism ; Genetic Pleiotropy ; Humans ; Proto-Oncogene Proteins p21(ras)/genetics ; Proto-Oncogene Proteins p21(ras)/metabolism ; Signal Transduction ; rac1 GTP-Binding Protein/genetics ; rac1 GTP-Binding Protein/metabolism
Chemical Substances	Calmodulin ; KRAS protein, human ; Proto-Oncogene Proteins p21(ras) (EC 3.6.5.2) ; rac1 GTP-Binding Protein (EC 3.6.5.2)
Language	English
Publishing date	2020-05-23
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms21103680
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Article ; Online: A mechanosensing mechanism controls plasma membrane shape homeostasis at the nanoscale.

Quiroga, Xarxa / Walani, Nikhil / Disanza, Andrea / Chavero, Albert / Mittens, Alexandra / Tebar, Francesc / Trepat, Xavier / Parton, Robert G / Geli, María Isabel / Scita, Giorgio / Arroyo, Marino / Le Roux, Anabel-Lise / Roca-Cusachs, Pere

eLife

2023 Volume 12

Abstract: As cells migrate and experience forces from their surroundings, they constantly undergo mechanical deformations which reshape their plasma membrane (PM). To maintain homeostasis, cells need to detect and restore such changes, not only in terms of overall ...

Abstract	As cells migrate and experience forces from their surroundings, they constantly undergo mechanical deformations which reshape their plasma membrane (PM). To maintain homeostasis, cells need to detect and restore such changes, not only in terms of overall PM area and tension as previously described, but also in terms of local, nanoscale topography. Here, we describe a novel phenomenon, by which cells sense and restore mechanically induced PM nanoscale deformations. We show that cell stretch and subsequent compression reshape the PM in a way that generates local membrane evaginations in the 100 nm scale. These evaginations are recognized by I-BAR proteins, which triggers a burst of actin polymerization mediated by Rac1 and Arp2/3. The actin polymerization burst subsequently re-flattens the evagination, completing the mechanochemical feedback loop. Our results demonstrate a new mechanosensing mechanism for PM shape homeostasis, with potential applicability in different physiological scenarios.
MeSH term(s)	Actins/metabolism ; Cell Membrane/metabolism ; Homeostasis
Chemical Substances	Actins
Language	English
Publishing date	2023-09-25
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.72316
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Article ; Online: Early proteostasis of caveolins synchronizes trafficking, degradation, and oligomerization to prevent toxic aggregation.

Morales-Paytuví, Frederic / Fajardo, Alba / Ruiz-Mirapeix, Carles / Rae, James / Tebar, Francesc / Bosch, Marta / Enrich, Carlos / Collins, Brett M / Parton, Robert G / Pol, Albert

The Journal of cell biology

2023 Volume 222, Issue 9

Abstract: Caveolin-1 (CAV1) and CAV3 are membrane-sculpting proteins driving the formation of the plasma membrane (PM) caveolae. Within the PM mosaic environment, caveola assembly is unique as it requires progressive oligomerization of newly synthesized caveolins ... ...

Abstract	Caveolin-1 (CAV1) and CAV3 are membrane-sculpting proteins driving the formation of the plasma membrane (PM) caveolae. Within the PM mosaic environment, caveola assembly is unique as it requires progressive oligomerization of newly synthesized caveolins while trafficking through the biosynthetic-secretory pathway. Here, we have investigated these early events by combining structural, biochemical, and microscopy studies. We uncover striking trafficking differences between caveolins, with CAV1 rapidly exported to the Golgi and PM while CAV3 is initially retained in the endoplasmic reticulum and laterally moves into lipid droplets. The levels of caveolins in the endoplasmic reticulum are controlled by proteasomal degradation, and only monomeric/low oligomeric caveolins are exported into the cis-Golgi with higher-order oligomers assembling beyond this compartment. When any of those early proteostatic mechanisms are compromised, chemically or genetically, caveolins tend to accumulate along the secretory pathway forming non-functional aggregates, causing organelle damage and triggering cellular stress. Accordingly, we propose a model in which disrupted proteostasis of newly synthesized caveolins contributes to pathogenesis.
MeSH term(s)	Caveolins/metabolism ; Proteostasis ; Caveolin 1/metabolism ; Membrane Proteins/metabolism ; Caveolae/metabolism ; Cell Membrane/metabolism ; Golgi Apparatus/metabolism
Chemical Substances	Caveolins ; Caveolin 1 ; Membrane Proteins
Language	English
Publishing date	2023-08-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202204020
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Article: Annexins: Ca

Enrich, Carlos / Rentero, Carles / Meneses-Salas, Elsa / Tebar, Francesc / Grewal, Thomas

Advances in experimental medicine and biology

2018 Volume 981, Page(s) 351–385

Abstract: Despite the discovery of annexins 40 years ago, we are just beginning to understand some of the functions of these still enigmatic proteins. Defined and characterized by their ability to bind anionic membrane lipids in a ... ...

Abstract	Despite the discovery of annexins 40 years ago, we are just beginning to understand some of the functions of these still enigmatic proteins. Defined and characterized by their ability to bind anionic membrane lipids in a Ca
MeSH term(s)	Animals ; Annexins/metabolism ; Calcium/metabolism ; Calcium Signaling/physiology ; Cell Membrane/metabolism ; Cell Movement/physiology ; Endocytosis/physiology ; Exocytosis/physiology ; Humans ; Lysosomes/metabolism ; Membrane Lipids/metabolism
Chemical Substances	Annexins ; Membrane Lipids ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2018-03-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ISSN	2214-8019 ; 0065-2598
ISSN (online)	2214-8019
ISSN	0065-2598
DOI	10.1007/978-3-319-55858-5_14
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Article ; Online: Annexin A6 and NPC1 regulate LDL-inducible cell migration and distribution of focal adhesions.

Jose, Jaimy / Hoque, Monira / Engel, Johanna / Beevi, Syed S / Wahba, Mohamed / Georgieva, Mariya Ilieva / Murphy, Kendelle J / Hughes, William E / Cochran, Blake J / Lu, Albert / Tebar, Francesc / Hoy, Andrew J / Timpson, Paul / Rye, Kerry-Anne / Enrich, Carlos / Rentero, Carles / Grewal, Thomas

Scientific reports

2022 Volume 12, Issue 1, Page(s) 596

Abstract: Cholesterol is considered indispensable for cell motility, but how physiological cholesterol pools enable cells to move forward remains to be clarified. The majority of cells obtain cholesterol from the uptake of Low-Density lipoproteins (LDL) and here ... ...

Abstract	Cholesterol is considered indispensable for cell motility, but how physiological cholesterol pools enable cells to move forward remains to be clarified. The majority of cells obtain cholesterol from the uptake of Low-Density lipoproteins (LDL) and here we demonstrate that LDL stimulates A431 squamous epithelial carcinoma and Chinese hamster ovary (CHO) cell migration and invasion. LDL also potentiated epidermal growth factor (EGF) -stimulated A431 cell migration as well as A431 invasion in 3-dimensional environments, using organotypic assays. Blocking cholesterol export from late endosomes (LE), using Niemann Pick Type C1 (NPC1) mutant cells, pharmacological NPC1 inhibition or overexpression of the annexin A6 (AnxA6) scaffold protein, compromised LDL-inducible migration and invasion. Nevertheless, NPC1 mutant cells established focal adhesions (FA) that contain activated focal adhesion kinase (pY397FAK, pY861FAK), vinculin and paxillin. Compared to controls, NPC1 mutants display increased FA numbers throughout the cell body, but lack LDL-inducible FA formation at cell edges. Strikingly, AnxA6 depletion in NPC1 mutant cells, which restores late endosomal cholesterol export in these cells, increases their cell motility and association of the cholesterol biosensor D4H with active FAK at cell edges, indicating that AnxA6-regulated transport routes contribute to cholesterol delivery to FA structures, thereby improving NPC1 mutant cell migratory behaviour.
MeSH term(s)	Animals ; Annexin A6/metabolism ; CHO Cells ; Carrier Proteins/metabolism ; Cell Line, Tumor ; Cell Movement ; Cholesterol, LDL/metabolism ; Cricetulus ; Focal Adhesions/metabolism ; Humans ; Membrane Proteins/metabolism ; Niemann-Pick C1 Protein/metabolism ; rab7 GTP-Binding Proteins/metabolism
Chemical Substances	Annexin A6 ; Carrier Proteins ; Cholesterol, LDL ; Membrane Proteins ; Niemann-Pick C1 Protein ; STARD3 protein, human ; rab7 GTP-Binding Proteins
Language	English
Publishing date	2022-01-12
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-021-04584-y
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Article ; Online: Annexin A6 improves anti-migratory and anti-invasive properties of tyrosine kinase inhibitors in EGFR overexpressing human squamous epithelial cells.

Hoque, Monira / Elmaghrabi, Yasmin A / Köse, Meryem / Beevi, Syed S / Jose, Jaimy / Meneses-Salas, Elsa / Blanco-Muñoz, Patricia / Conway, James R W / Swarbrick, Alexander / Timpson, Paul / Tebar, Francesc / Enrich, Carlos / Rentero, Carles / Grewal, Thomas

The FEBS journal

2020 Volume 287, Issue 14, Page(s) 2961–2978

Abstract: Annexin A6 (AnxA6), a member of the calcium ( ... ...

Abstract	Annexin A6 (AnxA6), a member of the calcium (Ca
MeSH term(s)	Animals ; Annexin A6/genetics ; Annexin A6/metabolism ; Apoptosis ; Carcinoma, Squamous Cell/drug therapy ; Carcinoma, Squamous Cell/metabolism ; Carcinoma, Squamous Cell/pathology ; Cell Movement ; Cell Proliferation ; ErbB Receptors/antagonists & inhibitors ; ErbB Receptors/metabolism ; Gene Expression Regulation, Neoplastic ; Humans ; Mice ; Neoplasm Invasiveness ; Neoplasms, Glandular and Epithelial/drug therapy ; Neoplasms, Glandular and Epithelial/metabolism ; Neoplasms, Glandular and Epithelial/pathology ; Phosphorylation ; Protein Kinase C-alpha/genetics ; Protein Kinase C-alpha/metabolism ; Protein Kinase Inhibitors/pharmacology ; Tumor Cells, Cultured ; Xenograft Model Antitumor Assays
Chemical Substances	Annexin A6 ; Protein Kinase Inhibitors ; EGFR protein, human (EC 2.7.10.1) ; ErbB Receptors (EC 2.7.10.1) ; Protein Kinase C-alpha (EC 2.7.11.13)
Language	English
Publishing date	2020-01-09
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.15186
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Article ; Online: Differential Regulation of RasGAPs in Cancer.

Grewal, Thomas / Koese, Meryem / Tebar, Francesc / Enrich, Carlos

Genes & cancer

2011 Volume 2, Issue 3, Page(s) 288–297

Abstract: Ever since their discovery as cellular counterparts of viral oncogenes more than 25 years ago, much progress has been made in understanding the complex networks of signal transduction pathways activated by oncogenic Ras mutations in human cancers. The ... ...

Abstract	Ever since their discovery as cellular counterparts of viral oncogenes more than 25 years ago, much progress has been made in understanding the complex networks of signal transduction pathways activated by oncogenic Ras mutations in human cancers. The activity of Ras is regulated by nucleotide exchange factors (GEFs) and GTPase activating proteins (GAPs), and much emphasis has been put into the biochemical and structural analysis of the Ras/GAP complex. The mechanisms by which GAPs catalyze Ras-GTP hydrolysis have been clarified and revealed that oncogenic Ras mutations confer resistance to GAPs and remain constitutively active. However, it is yet unclear how cells coordinate the large and divergent GAP protein family to promote Ras inactivation and ensure a certain biological response. Different domain arrangements in GAPs to create differential protein-protein and protein-lipid interactions are probably key factors determining the inactivation of the 3 Ras isoforms H-, K-, and N-Ras and their effector pathways. In recent years, in vitro as well as cell- and animal-based studies examining GAP activity, localization, interaction partners, and expression profiles have provided further insights into Ras inactivation and revealed characteristics of several GAPs to exert specific and distinct functions. This review aims to summarize knowledge on the cell biology of RasGAP proteins that potentially contributes to differential regulation of spatiotemporal Ras signaling.
Language	English
Publishing date	2011-07-14
Publishing country	United States
Document type	Journal Article
ZDB-ID	2538519-7
ISSN	1947-6027 ; 1947-6019
ISSN (online)	1947-6027
ISSN	1947-6019
DOI	10.1177/1947601911407330
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