L12: Mechanisms of Protein Action Flashcards
What is the approximate number of protein species in human cells due to gene variation and protein modification?
Around 1 million protein species.
Why is control of protein function crucial in human health?
Loss of protein control often leads to diseases, including cancer, due to the disruption of cellular pathways.
What is a kinase and why is it significant in cellular signaling?
A kinase is an enzyme that transfers phosphate groups to other proteins, playing a key role in signal transduction pathways.
What is allosteric regulation?
Allosteric regulation is when a molecule binds to a protein at a site other than the active site, causing a conformational change that affects the protein’s function.
Describe the BRAF V600 mutation and its effect on cell behavior.
The BRAF V600 mutation causes the BRAF protein to remain in an active state, leading to uncontrolled cell growth and cancer development.
How do mutations in the BRAF gene affect cancer development?
Mutations in BRAF can lock the protein in an active state, leading to constant cell growth signals and potentially contributing to cancer.
What is the role of polycystic kidney disease (PKD) proteins PKD1 and PKD2?
PKD1 and PKD2 are transmembrane proteins essential for kidney function and calcium signaling. Mutations cause abnormal kidney cell interactions, leading to cyst formation.
What is ubiquitination, and what role does it play in protein regulation?
Ubiquitination tags proteins for degradation by the proteasome, regulating protein levels and function in the cell.
How does haemophilia A relate to protein function?
Haemophilia A is caused by a deficiency in clotting factor VIII, leading to poor blood clotting and increased bleeding risk.
What is the significance of enzyme pathways in protein function?
Enzyme pathways, whether linear or amplifying, control how proteins interact to produce specific cellular outcomes, often regulated to meet the cell’s needs.
Describe feedback inhibition in enzyme pathways.
In feedback inhibition, the end product of a pathway binds to an enzyme in the pathway, changing its shape and halting further product formation.
What are protein interaction domains, and what is their function?
Protein interaction domains are structural areas that allow proteins to bind to others, facilitating scaffolding, localization, or regulation of protein activity.
How does the localization of proteins within a cell contribute to their regulation?
Proteins can be restricted to certain areas (like the nucleus or cytoplasm), allowing cells to control their activity based on location.
What is the role of phosphorylation in protein function?
Phosphorylation adds a phosphate group to a protein, often altering its activity, localization, or interactions with other proteins.
What is a GTPase and how does it function as a protein switch?
A GTPase is an enzyme that hydrolyzes GTP to GDP, toggling proteins between active and inactive states and controlling cellular processes like signaling.
What is protein hydroxylation, and what role does it play in cancer research?
Protein hydroxylation is the addition of an oxygen atom, which can affect protein function and has been studied in cancer for its role in tumor growth regulation.
How does the Ras protein act as a molecular switch in signaling pathways?
Ras binds GTP to become active and transmits growth signals; it becomes inactive when GTP is hydrolyzed to GDP.
What effect does calcium signaling have on protein localization?
Calcium levels can trigger proteins to move between the cytoplasm and nucleus, dynamically controlling their activity based on cellular signals.
Why are protein modifications like methylation and acetylation important?
They can regulate gene expression, protein stability, and interaction, adding complexity to cellular control mechanisms.
What are cyclin-dependent kinases, and what is their role in the cell cycle?
Cyclin-dependent kinases (CDKs) regulate cell cycle progression through phosphorylation, controlling key transitions such as mitosis.
What is competitive inhibition in enzyme regulation?
Competitive inhibition occurs when a molecule similar to the enzyme’s substrate binds to the active site, blocking the actual substrate and inhibiting enzyme activity.
How does haemoglobin exhibit allosteric regulation with oxygen?
When one oxygen molecule binds to haemoglobin, it increases the affinity of the remaining subunits for oxygen, facilitating oxygen binding in a stepwise manner.
What is proteolysis and how does it control protein function?
Proteolysis is the breakdown of proteins by proteases, often to regulate or eliminate proteins as part of cellular maintenance and signaling.
Explain the importance of pH in regulating protease activity, using cathepsin D as an example.
Cathepsin D is activated in acidic conditions, such as in lysosomes, allowing it to function in specific environments and preventing accidental protease activity in neutral pH areas like the cytoplasm.
