Zobrazeno 1 - 10
of 148
pro vyhledávání: '"Ivan, de Curtis"'
Autor:
Martina Ramella, Lucrezia Maria Ribolla, Sara Surini, Kristyna Sala, Diletta Tonoli, Jean-Michel Cioni, Arpan Kumar Rai, Lucas Pelkmans, Ivan de Curtis
Publikováno v:
iScience, Vol 27, Iss 4, Pp 109440- (2024)
Summary: Plasma membrane-associated platforms (PMAPs) form at specific sites of plasma membrane by scaffolds including ERC1 and Liprin-α1. We identify a mechanism regulating PMAPs assembly, with consequences on motility/invasion. Silencing Ser/Thr k
Externí odkaz:
https://doaj.org/article/809978cb03384d8f9c9ca1125e2054cb
Autor:
Marta Ripamonti, Andrea Lamarca, Norman E. Davey, Diletta Tonoli, Sara Surini, Ivan de Curtis
Publikováno v:
Communications Biology, Vol 5, Iss 1, Pp 1-12 (2022)
Liprin-α1 interacts with and recruits B56γ-PP2A at the front of migrating breast cancer cells, to promote cell protrusion and motility.
Externí odkaz:
https://doaj.org/article/c2df7b65cfde4ad79274e863b6867e83
Publikováno v:
Frontiers in Cell and Developmental Biology, Vol 10 (2022)
Focal adhesions are specialized integrin-dependent adhesion complexes, which ensure cell anchoring to the extracellular matrix. Focal adhesions also function as mechano-signaling platforms by perceiving and integrating diverse physical and (bio)chemi
Externí odkaz:
https://doaj.org/article/aef0dc5e2e9a4eb7ae3aff4c5348c202
Publikováno v:
Scientific Reports, Vol 8, Iss 1, Pp 1-14 (2018)
Abstract Depletion of liprin-α1, ERC1 or LL5 scaffolds inhibits extracellular matrix degradation by invasive cells. These proteins co-accumulate near invadosomes in NIH-Src cells, identifying a novel invadosome–associated compartment distinct from
Externí odkaz:
https://doaj.org/article/03f68b9343d147fab5c3d0fb2c1ff904
Publikováno v:
PLoS ONE, Vol 14, Iss 8, p e0220496 (2019)
The Rac1 and Rac3 GTPases are co-expressed in the developing nervous system, where they are involved in different aspects of neuronal development, including the formation of synapses. The deletion of both Rac genes determines a stronger reduction of
Externí odkaz:
https://doaj.org/article/9eb13eeda15946bc9d370e5789437d6f
Autor:
Sira A. Franchi, Romina Macco, Veronica Astro, Diletta Tonoli, Elisa Savino, Flavia Valtorta, Kristyna Sala, Martina Botta, Ivan de Curtis
Publikováno v:
Frontiers in Cellular Neuroscience, Vol 11 (2018)
Understanding the mechanisms guiding interneuron development is a central aspect of the current research on cortical/hippocampal interneurons, which is highly relevant to brain function and pathology. In this methodological study we have addressed th
Externí odkaz:
https://doaj.org/article/bb3661304bbd4907b819175d6f0e2b21
Publikováno v:
Oncogene
Liprins are a multifunctional family of scaffold proteins, identified by their involvement in several important neuronal functions related to signaling and organization of synaptic structures. More recently, the knowledge on the liprin family has exp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::617399a093fffbc287b34dc173961c33
https://doi.org/10.1038/s41388-021-02048-1
https://doi.org/10.1038/s41388-021-02048-1
Autor:
Ivan de Curtis
Publikováno v:
Cells, Vol 8, Iss 9, p 1063 (2019)
Rho family small guanosine triphosphatases (GTPases) are important regulators of the cytoskeleton, and are critical in many aspects of cellular and developmental biology, as well as in pathological processes such as intellectual disability and cancer
Externí odkaz:
https://doaj.org/article/503838052617486ba3b2e9c7609e32e3
Publikováno v:
Frontiers in Systems Neuroscience, Vol 8 (2014)
The proper function of the CNS requires the correct integration of glutamatergic neurons and GABAergic interneurons. Cortical GABAergic interneurons are characterized by extraordinary neurochemical and functional diversity. Although recent studies ha
Externí odkaz:
https://doaj.org/article/e02d3a3b3ae2437e9779265eb2fa2f94
Publikováno v:
PLoS ONE, Vol 9, Iss 4, p e93199 (2014)
GIT1 is an ArfGAP and scaffolding protein regulating cell adhesion and migration. The multidomain structure of GIT1 allows the interaction with several partners. Binding of GIT1 to some of its partners requires activation of the GIT1 polypeptide. Our
Externí odkaz:
https://doaj.org/article/6ee037d4006f4b94bead8c41d3b01c12