Cell Biology: Compartments and Protein Sorting
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Questions and Answers

What is the primary reason that biomolecular condensates are considered compartments?

  • They are formed through strong covalent bonds, creating a stable structure.
  • They allow for specific chemical reactions to occur within a concentrated space. (correct)
  • They are directly involved in the formation of new organelles.
  • They are surrounded by a selectively permeable membrane.
  • What is the main distinction between "condensation" and "aggregation" in the context of biomolecular condensates?

  • Aggregation involves covalent bonds, while condensation relies on weak interactions.
  • Condensation implies a specific arrangement of molecules with defined functions. (correct)
  • Aggregation involves a larger number of molecules.
  • Aggregation is a less dynamic process compared to condensation.
  • Why are the interactions between molecules within biomolecular condensates referred to as "weak interactions"?

  • They are easily disrupted by changes in temperature or pH.
  • They involve only hydrogen bonds, which are weaker than covalent bonds.
  • They are temporary and allow for dynamic interactions between molecules. (correct)
  • They are weaker than the interactions between molecules in the surrounding cytosol.
  • What is the role of "client" molecules in relation to biomolecular condensates?

    <p>They are attracted to the condensate and participate in cellular processes. (C)</p> Signup and view all the answers

    Which of the following is NOT a characteristic of biomolecular condensates?

    <p>They are always static and stable structures, providing a consistent environment for reactions. (A)</p> Signup and view all the answers

    What is a crucial requirement for the successful import of proteins during post-translational import?

    <p>Proteins must remain in an unfolded state. (D)</p> Signup and view all the answers

    Which class of proteins plays a significant role in maintaining the unfolded state of proteins during import?

    <p>Chaperones (B)</p> Signup and view all the answers

    What process occurs in the endoplasmic reticulum (ER) that contributes to membrane asymmetry?

    <p>Conjugation of GPI anchors to proteins (C)</p> Signup and view all the answers

    What role do chaperones play in post-translational protein import?

    <p>They keep proteins unfolded for membrane traversal. (D)</p> Signup and view all the answers

    What signifies the transport involved in the post-translational import process of proteins?

    <p>It requires active energy in the form of ATP. (D)</p> Signup and view all the answers

    What occurs when a protein is not correctly folded during its interaction with calnexin?

    <p>Another chaperone can bind to the protein. (B)</p> Signup and view all the answers

    What is the likely consequence if a protein accumulates excessively?

    <p>It may lead to the activation of the Unfolded Protein Response (UPR). (D)</p> Signup and view all the answers

    How does aggregation differ from forming condensates in proteins?

    <p>Aggregation is due to misfolded copies interacting, whereas condensates are organized structures. (C)</p> Signup and view all the answers

    What role does calnexin play during protein folding?

    <p>It assists in the binding of glucose to well-formed proteins. (B)</p> Signup and view all the answers

    What is indicated by the presence of one glucose molecule bound to calnexin?

    <p>The protein is well-formed and properly folded. (D)</p> Signup and view all the answers

    What is the primary function of disulfide bonds formed in the endoplasmic reticulum (ER)?

    <p>To stabilize proteins for extracellular exposure (A)</p> Signup and view all the answers

    Which type of glycosylation predominantly occurs in the endoplasmic reticulum (ER)?

    <p>N-glycosylation (D)</p> Signup and view all the answers

    What role does the chaperone protein calnexin serve in the ER?

    <p>It ensures proper protein folding (B)</p> Signup and view all the answers

    What is the significance of the sugar chains in N-glycosylation?

    <p>They act as molecular tags for protein processing (A)</p> Signup and view all the answers

    Why is calnexin named as such?

    <p>It is dependent on calcium for its function (D)</p> Signup and view all the answers

    Flashcards

    Calnexin Binding

    The interaction between calnexin and a protein indicating proper folding.

    Unfolded Protein Response (UPR)

    A cellular response triggered by misfolded proteins to restore normal function.

    Chaperone Function

    Proteins that assist in the proper folding of other proteins.

    Protein Aggregation

    The clumping together of misfolded proteins, often due to incorrect conformations.

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    Proteasome Activity

    The process of degrading and clearing misfolded proteins from the cell.

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    Biomolecular condensate

    A compartment of concentrated molecules not enclosed by a membrane.

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    Chemical reactions in condensates

    Biomolecular condensates allow for chemical reactions to occur within them.

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    Weak interactions

    Transient associations between molecules in a biomolecular condensate.

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    Client molecules

    Molecules attracted to condensates due to affinity or binding interactions.

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    Dynamism of molecules

    Molecules within biomolecular condensates are constantly interacting and in motion.

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    Disulfide bonds

    Covalent bonds that stabilize protein structure by connecting cysteine residues.

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    Glycosylation

    The process of adding sugar molecules to proteins, crucial for folding and function.

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    N-glycosylation

    Type of glycosylation where sugar is attached to asparagine residues in proteins.

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    Calnexin

    A chaperone protein that helps ensure proper protein folding in the ER.

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    ER functions

    Key cellular processes such as disulfide bond formation and glycosylation occur in the ER.

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    Post-Translational Import

    Import of proteins into organelles while they are still unfolded and immature.

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    Role of Chaperones

    Proteins that assist in maintaining unfolded states or correct folding of other proteins.

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    ATP-Dependent Transport

    Process requiring ATP energy to transport proteins across membranes actively.

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    GPI Anchors

    Glycosylphosphatidylinositol anchors help attach proteins to membranes.

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    Compartmentalization in ER

    Separation of biochemical reactions in the endoplasmic reticulum for efficiency.

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    Study Notes

    Cell Compartments and Protein Sorting

    • Cells compartmentalize to ensure materials reach the correct location at the right time, facilitated by transport systems
    • Compartments restrict reactions by concentrating enzymes, substrates, and regulators
    • Compartments increase membrane surface area for reactions like oxidative phosphorylation
    • Membranes are generally impermeable so specialized transport mechanisms are essential for molecules to enter/interact with compartments

    Intracellular Compartments

    • Nucleus and cytosol (connected by pore complexes)
    • Organelles in secretory/endocytic pathways (ER, Golgi, endosomes, lysosomes, peroxisomes)
    • Mitochondria

    Membrane Types in Cells

    • Table 12-2: Shows relative amounts of membrane types in liver hepatocytes and pancreatic exocrine cells
    • Plasma membrane
    • Rough ER membrane
    • Smooth ER membrane
    • Golgi apparatus membrane
    • Mitochondrial membranes (outer and inner)
    • Nucleus membrane (outer/inner)
    • Lysosome membrane
    • Peroxisome membrane
    • Endosome membrane

    Compartmentalization within Cells

    • Various organelles occupy different percentages of cell volume (cytosol, mitochondria, rough ER, smooth ER, Golgi, nucleus, peroxisomes, lysosomes, endosomes)
    • The relationship between volume and surface area of different cell compartments is not always proportional, allowing for varied functions in different types of cells.

    Electron Microscopy

    • Electron microscopy images of organelles/cell structures can be misleading due to artifacts rather than actual structures.
    • Electron-dense materials absorb more electrons in electron microscopy, showing up darker.
    • Examples include lysosomes and other densely packed structures

    Membrane-Bound Organelles and Biomolecular Condensates

    • Organelles are primarily membrane-bound structures: mitochondria, nucleus, lysosomes
    • Biomolecular condensates are compartments without membranes but still function as distinct cellular structures.

    Vesicle Transport Principles

    • Vesicle transport is highly regulated in both time and space, involving polarization of membranes.
    • Orientation/polarity of membranes is crucial in vesicle transport (lumen of vesicle versus outer environment.)
    • Polarization of membranes is critical for vesicle interactions during transport between organelles.

    Protein Transport and Translocation

    • Proteins destined for organelles have specific signal sequences (typically amino acid stretches).
    • Co-translational transport: ribosomes attach to ER membrane as proteins synthesize, directly inserting nascent proteins into the ER lumen or membrane
    • Post-translational transport: proteins are fully synthesized in the cytosol before being imported into the organelle such as ER or mitochondria utilizing distinct methods.

    Endoplasmic Reticulum (ER)

    • ER is involved in protein synthesis and processing (co-translational and post-translational)
    • Contains translocon complexes essential for protein import.
    • Contains chaperone proteins (e.g., calnexin) that assist in protein folding and quality control.

    Signal Recognition Particle (SRP) and Protein Import

    • SRP binds to signal sequence of nascent proteins, pausing translation until ribosome docks on the ER membrane.
    • Receptor and ribosome facilitate protein import via the translocon (channel) into ER lumen.
    • This process is dynamic and regulated to ensure efficient protein targeting.

    Polyribosomes/Polysomes

    • Clusters of ribosomes that simultaneously translate a single mRNA molecule.
    • Efficient synthesis of multiple copies of protein.

    Unfolded Protein Response (UPR)

    • Cells respond to misfolded proteins in the ER by initiating UPR (three branches)
    • UPR: aims to restore normal function but not necessarily exclude other mechanisms
    • Misfolded proteins exit ER or are cleared via proteasomes for degradation (energy dependence).
    • Proteasome: a protein complex not surrounded by membranes; it is a complex structure with specific functions for protein degradation.

    Peroxisomes.

    • Peroxisomes are membrane-bound organelles involved in detoxification (beta-oxidation, production of hydrogen peroxide-conversion to water), lipid metabolism and synthesis of certain lipids (e.g., plasmalogens).
    • Peroxisomes form de novo through vesicle fusion (distinct from organelle division).
    • Peroxin (PEX) proteins: transport essential fatty acids and enzymes.

    Protein Transport: Mitochondria

    • Mitochondria require substantial protein import due to their limited genome
    • Use different translocator complexes (TOM, TIM, OXA) to import proteins, requiring energy.
    • Protein import processes are selective due to signal sequences and translocator proteins.

    Nuclear Transport

    • Nuclear envelope has nuclear pores to allow selective transport of proteins/RNA/nucleotides between nucleus and cytosol.
    • Gated regulated transport of materials (e.g., histones, RNA, proteins, nucleotides) through the nuclear pores
    • Signal sequences/import receptors guide proteins through nuclear pores.
    • Nuclear transport is energy-dependent (using small GTPase Ran).

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    Description

    Explore the intricate structures and functions of cell compartments and their role in protein sorting. This quiz covers intracellular compartment structures, membrane types, and the essential transport mechanisms that maintain cellular integrity. Test your knowledge on how cells compartmentalize processes to optimize their functions.

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