8 results on '"Paulina, Moreno-Layseca"'
Search Results
2. Integrin trafficking in cells and tissues
- Author
-
Jaroslav Icha, Hellyeh Hamidi, Johanna Ivaska, and Paulina Moreno-Layseca
- Subjects
Integrins ,Protein family ,Integrin ,Endocytic cycle ,Endocytosis ,Models, Biological ,Article ,Extracellular matrix ,03 medical and health sciences ,0302 clinical medicine ,Cell Movement ,Cell Adhesion ,Animals ,Humans ,Cell adhesion ,030304 developmental biology ,0303 health sciences ,biology ,Chemistry ,Cell Membrane ,Cell Biology ,Cell biology ,Transport protein ,Protein Transport ,030220 oncology & carcinogenesis ,biology.protein ,Signal transduction ,Signal Transduction - Abstract
Cell adhesion to the extracellular matrix is fundamental to metazoan multicellularity and is accomplished primarily through the integrin family of cell-surface receptors. Integrins are internalized and enter the endocytic-exocytic pathway before being recycled back to the plasma membrane. The trafficking of this extensive protein family is regulated in multiple context-dependent ways to modulate integrin function in the cell. Here, we discuss recent advances in understanding the mechanisms and cellular roles of integrin endocytic trafficking.
- Published
- 2019
3. Cargo-specific recruitment in clathrin and dynamin-independent endocytosis
- Author
-
Christian Sommer, Roosa E. Kallionpää, Satyajit Mayor, Stefan Linder, Stefan Veltel, Guillaume Jacquemet, Pauliina Kronqvist, Johanna Ivaska, Pasquale Cervero, Paulina Moreno-Layseca, James Rae, Martin Aepfelbacher, Niklas Z. Jäntti, Giorgio Scita, Hussein Al-Akhrass, Robert G. Parton, Andrea Disanza, Matthias Selbach, Rashmi Godbole, and Leticia Oliveira-Ferrer
- Subjects
biology ,Chemistry ,media_common.quotation_subject ,Endocytic cycle ,Integrin ,Endocytosis ,Clathrin ,Cell biology ,biology.protein ,Internalization ,Actin ,Tissue homeostasis ,Dynamin ,media_common - Abstract
Spatially controlled, cargo-specific endocytosis is essential for development, tissue homeostasis, and cancer invasion and is often hijacked by viral infections 1. Unlike clathrin-mediated endocytosis, which exploits cargo-specific adaptors for selective protein internalization, the clathrin and dynamin-independent endocytic pathway (CLIC-GEEC, CG-pathway) has until now been considered a bulk internalization route for the fluid phase, glycosylated membrane proteins and lipids 2,3. Although the core molecular players of CG endocytosis have been recently defined, no cargo-specific adaptors are known and evidence of selective protein uptake into the pathway is lacking 3. Here, we identify the first cargo-specific adaptor for CG-endocytosis and demonstrate its clinical relevance in breast cancer progression. By combining unbiased molecular characterization and super-resolution imaging, we identified the actin-binding protein swiprosin-1 (EFHD2) as a cargo-specific adaptor regulating integrin internalization via the CG-pathway. Swiprosin-1 couples active Rab21-associated integrins with key components of the CG-endocytic machinery, IRSp53 and actin. Swiprosin-1 is critical for integrin endocytosis, but not for other CG-cargo and supports integrin-dependent cancer cell migration and invasion, with clinically relevant implications for breast cancer. Our results demonstrate a previously unknown cargo selectivity for the CG-pathway and opens the possibility to discover more adaptors regulating it.
- Published
- 2020
4. Cargo-specific recruitment in clathrin- and dynamin-independent endocytosis
- Author
-
Paulina, Moreno-Layseca, Niklas Z, Jäntti, Rashmi, Godbole, Christian, Sommer, Guillaume, Jacquemet, Hussein, Al-Akhrass, James R W, Conway, Pauliina, Kronqvist, Roosa E, Kallionpää, Leticia, Oliveira-Ferrer, Pasquale, Cervero, Stefan, Linder, Martin, Aepfelbacher, Henrik, Zauber, James, Rae, Robert G, Parton, Andrea, Disanza, Giorgio, Scita, Satyajit, Mayor, Matthias, Selbach, Stefan, Veltel, and Johanna, Ivaska
- Subjects
Dynamins ,Cell Movement ,rab GTP-Binding Proteins ,Integrin beta1 ,Intracellular Signaling Peptides and Proteins ,Humans ,Biological Transport ,Breast Neoplasms ,Female ,Actins ,Clathrin ,Endocytosis - Abstract
Spatially controlled, cargo-specific endocytosis is essential for development, tissue homeostasis and cancer invasion. Unlike cargo-specific clathrin-mediated endocytosis, the clathrin- and dynamin-independent endocytic pathway (CLIC-GEEC, CG pathway) is considered a bulk internalization route for the fluid phase, glycosylated membrane proteins and lipids. While the core molecular players of CG-endocytosis have been recently defined, evidence of cargo-specific adaptors or selective uptake of proteins for the pathway are lacking. Here we identify the actin-binding protein Swiprosin-1 (Swip1, EFHD2) as a cargo-specific adaptor for CG-endocytosis. Swip1 couples active Rab21-associated integrins with key components of the CG-endocytic machinery-Arf1, IRSp53 and actin-and is critical for integrin endocytosis. Through this function, Swip1 supports integrin-dependent cancer-cell migration and invasion, and is a negative prognostic marker in breast cancer. Our results demonstrate a previously unknown cargo selectivity for the CG pathway and a role for specific adaptors in recruitment into this endocytic route.
- Published
- 2020
5. The requirement of integrins for breast epithelial proliferation
- Author
-
Amber Wood, Ahmet Ucar, Paulina Moreno-Layseca, Heyuan Sun, Charles H. Streuli, Safiah Olabi, Keith Brennan, and Andrew P. Gilmore
- Subjects
rac1 GTP-Binding Protein ,0301 basic medicine ,Integrin beta Chains ,Histology ,Cell division ,Receptor, ErbB-2 ,oncogenes ,proliferation ,Integrin ,Breast Neoplasms ,medicine.disease_cause ,Cell Line ,Pathology and Forensic Medicine ,Malignant transformation ,Small hairpin RNA ,Extracellular matrix ,Mice ,03 medical and health sciences ,mammary epithelial cells ,medicine ,Animals ,Humans ,Mammary Glands, Human ,Protein kinase B ,Cells, Cultured ,Cell Proliferation ,biology ,Oncogene ,Neuropeptides ,Epithelial Cells ,Cell Biology ,General Medicine ,Cell biology ,Cell Transformation, Neoplastic ,030104 developmental biology ,Beta1-integrin ,p21-Activated Kinases ,biology.protein ,Female ,Carcinogenesis ,Proto-Oncogene Proteins c-akt ,Cell Division ,Signal Transduction - Abstract
Epithelial cells forming mammary gland ducts and alveoli require adhesion to the extracellular matrix for their function. Mammary epithelial cells need β1-integrins for normal cell cycle regulation. However, the role of β1-integrins in tumorigenesis has not been fully resolved. β1-integrin is necessary for tumour formation in transgenic mice expressing the Polyomavirus Middle T antigen, but it is dispensable in those overexpressing ErbB2. This suggests that some oncogenes can manage without β1-integrin to proliferate and form tumours, while others still require it. Here we have developed a model to test whether expression of an oncogene can surpass the need for β1-integrin to drive proliferation. We co-expressed the ErbB2 or Akt oncogenes with shRNA to target β1-integrin in mammary epithelial cells, and found that they show a differential dependence on β1-integrin for cell division. Moreover, we identified a key proliferative role of the Rac1-Pak axis downstream of β1-integrin signalling. Our data suggest that, in mammary epithelial cells, oncogenes with the ability to signal to Pak surpass the requirement of integrins for malignant transformation. This highlights the importance of using the correct combination therapy for breast cancer, depending on the oncogenes expressed in the tumour.
- Published
- 2017
6. Specific β-containing Integrins Exert Differential Control on Proliferation and Two-dimensional Collective Cell Migration in Mammary Epithelial Cells
- Author
-
Alexa I. Jeanes, Nasreen Akhtar, Ricky Tsang, Pengbo Wang, Paulina Moreno-Layseca, Julia Cheung, Charles H. Streuli, Nikki R. Paul, Fiona M Foster, and Keith Brennan
- Subjects
Male ,Cellular differentiation ,Immunoblotting ,Integrin ,RAC1 ,Real-Time Polymerase Chain Reaction ,Biochemistry ,Cell Line ,Focal adhesion ,Extracellular matrix ,Mice ,03 medical and health sciences ,Mammary Glands, Animal ,0302 clinical medicine ,Cell Movement ,Pregnancy ,Cell Adhesion ,Animals ,Cell adhesion ,Molecular Biology ,Cells, Cultured ,Cell Proliferation ,030304 developmental biology ,0303 health sciences ,biology ,Adhesome ,Mammary Gland ,Integrin beta1 ,Cell Cycle ,Cell Differentiation ,Cell Biology ,Cell cycle ,Flow Cytometry ,Cell biology ,Epithelial cell ,030220 oncology & carcinogenesis ,biology.protein ,Female ,Signal Transduction - Abstract
Background: Integrin-mediated ECM adhesion is required for mammary epithelial proliferation, but the mechanism is not known. Results: Gene deletion studies show that β1-integrin-null mammary epithelial cells retain β3-integrins and the ability to undergo two-dimensional migration, and Rac1 rescues their proliferation defect. Conclusion: β1-Integrins uniquely control proliferation in mammary cells via Rac1, whereas β3-integrins support two-dimensional migration. Significance: Specific β-integrin-containing adhesions determine different cell-fate responses., Understanding how cell cycle is regulated in normal mammary epithelia is essential for deciphering defects of breast cancer and therefore for developing new therapies. Signals provided by both the extracellular matrix and growth factors are essential for epithelial cell proliferation. However, the mechanisms by which adhesion controls cell cycle in normal epithelia are poorly established. In this study, we describe the consequences of removing the β1-integrin gene from primary cultures of mammary epithelial cells in situ, using CreER. Upon β1-integrin gene deletion, the cells were unable to progress efficiently through S-phase, but were still able to undergo collective two-dimensional migration. These responses are explained by the presence of β3-integrin in β1-integrin-null cells, indicating that integrins containing different β-subunits exert differential control on mammary epithelial proliferation and migration. β1-Integrin deletion did not inhibit growth factor signaling to Erk or prevent the recruitment of core adhesome components to focal adhesions. Instead the S-phase arrest resulted from defective Rac activation and Erk translocation to the nucleus. Rac inhibition prevented Erk translocation and blocked proliferation. Activated Rac1 rescued the proliferation defect in β1-integrin-depleted cells, indicating that this GTPase is essential in propagating proliferative β1-integrin signals. These results show that β1-integrins promote cell cycle in mammary epithelial cells, whereas β3-integrins are involved in migration.
- Published
- 2012
7. Signalling pathways linking integrins with cell cycle progression
- Author
-
Charles H. Streuli and Paulina Moreno-Layseca
- Subjects
MAPK/ERK pathway ,Cell type ,Integrins ,biology ,Growth factor ,medicine.medical_treatment ,Integrin ,Cancer ,Cell Cycle Checkpoints ,medicine.disease ,Cell biology ,Extracellular Matrix ,Extracellular matrix ,Fibrosis ,medicine ,biology.protein ,Cell Adhesion ,Humans ,Molecular Biology ,Protein kinase B ,Cell Proliferation ,Signal Transduction - Abstract
Integrins are adhesion receptors that allow cells to sense and respond to microenvironmental signals encoded by the extracellular matrix. They are crucial for the adhesion, survival, proliferation, differentiation and migration of most cell types. In cell cycle regulation, integrin-mediated signals from the local niche constitute a spatial checkpoint to allow cells to progress from G1 to S phase, and are as important as temporal growth factor signals. Proliferation is altered in diseases such as cancer and fibrosis, so understanding how integrins contribute to this process will provide novel strategies for therapy. Here we consider recent studies to elucidate mechanisms of integrin-dependent cell cycle progression and discuss perspectives for future study.
- Published
- 2013
8. Serotonin receptor 5-HT5A in rat hippocampus decrease by leptin treatment
- Author
-
Jesica Escobar, Laura C. Berumen, Angelina Rodríguez, Guadalupe García-Alcocer, Ricardo Miledi, and Paulina Moreno-Layseca
- Subjects
Leptin ,Male ,medicine.medical_specialty ,Serotonin ,Neurogenesis ,Hippocampus ,Down-Regulation ,Hippocampal formation ,Biology ,Synaptic Transmission ,Rats, Sprague-Dawley ,chemistry.chemical_compound ,Internal medicine ,medicine ,Animals ,Neurotransmitter ,Receptor ,5-HT receptor ,General Neuroscience ,Dentate gyrus ,Rats ,Endocrinology ,chemistry ,Gene Expression Regulation ,Receptors, Serotonin ,Dentate Gyrus ,Injections, Intraperitoneal - Abstract
Hydroxytryptamine (5-HT) is involved in a variety of different physiological processes and behaviors through the activation of equally diverse receptors subtypes. In this work we studied the changes on the expression of 5-HT5A receptors in rat hippocampus induced by leptin, an adipocyte-derived hor- mone that has been reported to participate in the modulation of food intake and in adult hippocampal neurogenesis. To study the effect of leptin on the 5-HT5A receptor gene expression a qRT-PCR was used and the distribution of those receptors in the hippocampus was visualized by immunohistochemistry. Rats were separated in four groups: control (untreated rats), leptin-treated, serotonin-treated and lep- tin + serotonin treated. The results showed that even though the 5-HT5A gene expression did not change in the hippocampus of any of the treated groups, in the rats treated with leptin and serotonin, the specific immunostaining for the 5-HT5A serotonin receptor decreased significantly in the dentate gyrus. © 2010 Elsevier Ireland Ltd. All rights reserved.
- Published
- 2010
Catalog
Discovery Service for Jio Institute Digital Library
For full access to our library's resources, please sign in.