Scs2p Protein
Scs2p Protein - Related Videos
08:46
Green Fluorescent Protein-based Expression Screening of Membrane Proteins in Escherichia coli
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Cited by 34 •
2015
A streamlined approach to screening for the expression of recombinant membrane proteins in Escherichia coli based on fusion to green fluorescent protein is presented.
06:26
Rapid Assessment of Membrane Protein Quality by Fluorescent Size Exclusion Chromatography
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Cited by 2 •
2023
The present protocol describes a procedure to perform fluorescent size exclusion chromatography (FSEC) on membrane proteins to assess their quality for downstream functional and structural analysis. Representative FSEC results collected for several G-protein coupled receptors (GPCRs) under detergent-solubilized and detergent-free conditions are presented.
07:47
Staining of Proteins in Gels with Coomassie G-250 without Organic Solvent and Acetic Acid
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Cited by 94 •
2009
A short protocol for protein staining with Coomassie Brilliant Blue (CBB) G-250 in polyacrylamide gels is described without using organic solvents or acetic acid as in the classical staining procedures with CBB.
02:04
Protein-protein Interfaces
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2020
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
02:26
Conservation of Protein Domains Over Different Proteins
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2020
Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms. A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
FAQs
The cytosolic MSP domain recognizes FFAT motifs, short sequence features present in particular interaction partners. This recognition gives Scs2p a selective way to associate with proteins that participate in membrane-contact functions. Because the same protein also contains a membrane anchor, those partners become positioned at the ER surface rather than remaining distributed throughout the cytosol, supporting localized interorganelle communication.
The membrane anchor keeps Scs2p embedded in the ER and stabilizes its association with FFAT-motif-containing proteins at contact sites. Binding alone would not provide the same spatial organization if the interaction partners could diffuse away from the ER. Retention therefore connects molecular recognition in the cytosol with the physical arrangement needed for lipid handling and organelle coordination.
These two regions provide complementary functions. The MSP domain supplies the interaction interface for FFAT-motif-containing proteins, whereas the membrane anchor fixes Scs2p to the ER membrane. Their cooperation creates a tethering arrangement that brings selected proteins to a defined membrane location. This combined mechanism links protein recruitment with contact-site organization, allowing membrane-associated processes to occur in a coordinated setting.
Scs2p offers a budding-yeast model for examining VAP-family proteins and the principles governing membrane contact sites. Its defined combination of an MSP domain and ER membrane anchor makes it possible to relate partner binding to membrane organization. Findings from this system help frame how contact-site proteins may coordinate lipid distribution, signaling, and communication between organelles in eukaryotic cells.
Investigations of Scs2p can focus on lipid transport, phosphoinositide metabolism, and communication between organelles. These processes are connected because membranes must exchange or regulate components while preserving cellular organization. Examining how Scs2p recruits and retains interaction partners helps researchers relate contact-site structure to broader aspects of cellular homeostasis, rather than treating lipid movement or signaling as isolated events.
Scs2p can be used to examine how a membrane-bound organizer links molecular interactions to the positioning of proteins at ER contact sites. Its FFAT-motif-dependent binding highlights the role of partner recognition, while its ER retention highlights spatial control. Together, these features provide a framework for analyzing how membrane contacts support coordinated activity between distinct cellular compartments.
Although Scs2p is studied in budding yeast, it is relevant to broader biology because it models VAP-family proteins and membrane contact sites. The associated principles concern lipid distribution, signaling, organelle communication, and cellular homeostasis, all of which are general eukaryotic concerns. Thus, the system connects a tractable yeast model with questions about how cells coordinate multiple membranes.