P120-catenin
P120-catenin - Related Videos
01:23
Catenins
0 Views •
2023
Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins. Catenins in Cell Junctions Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the adherens...
09:41
Reconstitution Of β-catenin Degradation In Xenopus Egg Extract
0 Views •
Cited by 4 •
2014
A method is described for analyzing protein degradation using radiolabeled and luciferase-fusion proteins in Xenopus egg extract and its adaptation for high-throughput screening for small molecule modulators of protein degradation.
15:13
Structure-function Studies in Mouse Embryonic Stem Cells Using Recombinase-mediated Cassette Exchange
0 Views •
Cited by 6 •
2017
Proteins often contain multiple domains that can exert different cellular functions. Gene knock-outs (KO) do not consider this functional diversity. Here, we report a recombination-mediated cassette exchange (RMCE)-based structure-function approach in KO embryonic stem cells that allows for the molecular dissection of various functional domains or variants of a protein.
10:13
A Multiplexed Luciferase-based Screening Platform for Interrogating Cancer-associated Signal Transduction in Cultured Cells
0 Views •
Cited by 6 •
2013
Achieving a systems level understanding of cellular processes is a goal of modern-day cell biology. We describe here strategies for multiplexing luciferase reporters of various cellular function end-points to interrogate gene function using genome-scale RNAi libraries.
06:17
Measuring Protein Binding to F-actin by Co-sedimentation
0 Views •
Cited by 18 •
2017
This protocol describes a method to test the ability of a protein to co-sediment with filamentous actin (F-actin) and, if binding is observed, to measure the affinity of the interaction.
FAQs
Binding to the cadherin cytoplasmic tail helps p120-catenin keep cadherins at the plasma membrane rather than allowing their internalization and degradation. This stabilizing effect preserves the molecular components needed for adhesion between neighboring cells. Consequently, changes that reduce this association can weaken cell-cell contacts and contribute to disrupted tissue organization.
The armadillo-repeat region provides the structural context for p120-catenin’s interaction with the cadherin tail. That interaction connects a membrane adhesion molecule with intracellular regulation, allowing cadherin stability and signaling to be considered together rather than as separate events. This coupling helps explain how membrane-localized protein interactions influence broader tissue behavior.
p120-catenin influences Rho-family GTPases, which regulate actin-cytoskeleton dynamics. Because actin organization affects how cells maintain contacts and coordinate movement, this signaling connection gives p120-catenin effects beyond cadherin retention. The result is a mechanistic link between adhesion, cytoskeletal behavior, and changes in cell positioning or tissue remodeling.
Localization indicates where p120-catenin can interact with cadherins and influence adhesion-related signaling. At the plasma membrane, its association supports cadherin stability; altered localization may therefore coincide with weaker contacts, impaired epithelial barrier function, or changed polarity. Examining distribution is consequently important when interpreting tissue architecture and cell-cell organization.
Its effects on adhesion, polarity, barrier function, and coordinated movement make it relevant to how tissues form and reorganize during development. Studying p120-catenin can connect molecular changes at cadherin-based contacts with larger patterns of tissue architecture. The same framework also supports investigations of tissue remodeling, where cells must maintain or change contacts.
Altered p120-catenin expression or localization can weaken cell adhesion and modify signaling through Rho-family GTPases. These changes provide a biological context for examining how tissue organization and coordinated cell behavior become disrupted. In cancer research, the protein is therefore relevant as a link between adhesion status, cytoskeletal regulation, and altered tissue architecture.