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What role do transport vesicles play in eukaryotic cells?
What role do transport vesicles play in eukaryotic cells?
Which of the following organelles are isolated from the vesicular traffic in eukaryotic cells?
Which of the following organelles are isolated from the vesicular traffic in eukaryotic cells?
What structure is characterized by its ribosome-studded membrane and is involved in the secretion of digestive enzymes?
What structure is characterized by its ribosome-studded membrane and is involved in the secretion of digestive enzymes?
How do organelles communicate with the cell exterior?
How do organelles communicate with the cell exterior?
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What is the primary function of the endoplasmic reticulum (ER) in eukaryotic cells?
What is the primary function of the endoplasmic reticulum (ER) in eukaryotic cells?
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What are microsomes derived from after homogenization of tissues or cells?
What are microsomes derived from after homogenization of tissues or cells?
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What distinguishes rough microsomes from smooth microsomes?
What distinguishes rough microsomes from smooth microsomes?
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What do membrane-bound ribosomes primarily synthesize?
What do membrane-bound ribosomes primarily synthesize?
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How do scientists typically separate rough and smooth microsomes?
How do scientists typically separate rough and smooth microsomes?
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What is a polyribosome?
What is a polyribosome?
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What is a characteristic of the nucleolus?
What is a characteristic of the nucleolus?
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How does the total membrane surface area of the endoplasmic reticulum in liver and pancreatic cells compare to the plasma membrane?
How does the total membrane surface area of the endoplasmic reticulum in liver and pancreatic cells compare to the plasma membrane?
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What was a major evolutionary event in the formation of early eukaryotic cells?
What was a major evolutionary event in the formation of early eukaryotic cells?
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What is the relationship of the lumen of internal compartments in eukaryotic cells to the extracellular space?
What is the relationship of the lumen of internal compartments in eukaryotic cells to the extracellular space?
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During the evolution of eukaryotic cells, what was the fate of the endosymbiont?
During the evolution of eukaryotic cells, what was the fate of the endosymbiont?
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Study Notes
Intracellular Organization and Protein Sorting
- The thousands of macromolecules and biochemical activities in a cell are spatially organized into different regions.
- Eukaryotic cells are subdivided into membrane-enclosed compartments (organelles) unlike bacteria.
- Key organelles include the endoplasmic reticulum, Golgi apparatus, lysosomes, plastids, and mitochondria.
- Some organelles are further subcompartmentalized by internal membranes.
- Biomolecular condensates (reversible assemblies) are specialized factories or temporary storage depots.
- The nucleolus is an example of a biomolecular condensate, not enclosed by a membrane.
Animal Cell Protein Molecules
- An animal cell contains about 10 billion protein molecules (perhaps 10,000 kinds).
- Protein synthesis almost always begins in the cytosol (cytoplasm outside membrane-enclosed organelles).
- Newly synthesized proteins are delivered to the specific organelles needing them.
- Organelles have a unique protein and lipid composition to guide protein and lipid delivery.
Compartmentalization of Cells
- Intracellular membrane systems create enclosed compartments separate from the cytosol.
- This compartmentalization creates specialized aqueous spaces.
- Subsets of molecules (proteins, reactants, ions) are concentrated in these spaces to optimize biochemical reactions.
- Multiple types of compartments allow simultaneous biochemical reactions needing distinct conditions.
Relative Volumes of Intracellular Compartments in a Liver Cell
- Cytosol occupies 54% of the total cell volume.
- Mitochondria occupy 22%.
- Rough ER cisternae occupy 9%.
- Smooth ER cisternae occupy 5%.
- Golgi cisternae occupy 6%.
- Nucleus occupies 1%.
- Peroxisomes occupy 1%.
- Lysosomes occupy 1%.
- Endosomes occupy 1%.
Relative Amounts of Membrane Types
- In liver cells, plasma membrane constitutes only 2% of the total cell membrane.
- Rough ER membrane makes up 35%.
- Smooth ER membrane makes up 16%.
- Golgi apparatus makes up 7%.
- Intermediate filaments, microtubule, Mitochondria, secretory vesicle, lysosomes, peroxisomes, and endosomes membranes are present in significant amounts in liver cells as well. The percentage differs in cells of other tissues.
Evolutionary Origins of Organelles
- Eukaryotic cells likely arose from the joining of an ancient anaerobic archaeon and aerobic bacterium.
- Membrane expansion through protrusions and blebs may have stabilized the nascent nuclear pores.
- The added surface area facilitated metabolite exchange.
- Symbiotic relationship with the aerobic bacterium allowed the archaeon to increase in volume.
Topological Relationships of Organelles
- The lumen of internal compartments are topologically equivalent to extracellular space.
- Endosymbionts (evolved into mitochondria) escaped the enclosing membrane.
- Expanded compartments became specialized in modern-day eukaryotic cells.
- Cytosol and nucleus were originally the same.
Topologically Equivalent Compartments
- Compartments were derived from the same primordial internal compartment.
- Compartments can exchange material with one another via vesicular transport pathways; these pathways are consistent amongst cells.
Topologically Equivalent Pathways
- Molecules can be transferred between compartments by transport vesicles.
- Membrane budding and fusion permit communication between organelles and the cell's exterior.
Major Intracellular Compartments
- Nucleus and cytosol (topologically equivalent).
- Organelles in the secretory and endocytic pathways: ER and Golgi, endosomes, lysosomes, and transport vesicles.
- Endosymbiont-derived organelles: mitochondria and, in plants, plastids.
Macromolecules Segregated Without Membranes
- Macromolecule subsets can segregate within cells without a membrane barrier.
- Nucleic acids or proteins can act as scaffolds in biomolecular condensates.
- Scaffold molecules attract client molecules in a concentrated region.
- Client molecules do not diffuse away readily under high concentration of binding sites for clients.
Examples of Biomolecular Condensates
- Nucleolus (rRNA and ribosome assembly).
- Pyrenoid (carbon fixation in algae).
- Stress granules (temporary storage).
- P-granules (RNA metabolism).
- Balbiani body (RNA and organelle localization).
- Cajal body (mRNA processing).
- Paraspeckles (regulation of gene expression).
- RNA transport granule (RNA localization).
- PML body (regulation of gene expression).
- Postsynaptic density (neuronal transmission).
Biomolecular Condensates as Biochemical Factories
- Some condensates concentrate molecules for specific biochemical reactions.
- Condensates are used for temporary storage and specialized chemical processes.
- Examples from various cell types.
Biomolecular Condensates Form and Disassemble
- Weak interactions are necessary for condensate formation and stability from a well-mixed system.
- Changes in interaction strength can influence condensate properties (formation and physical properties).
- The change can regulate the biological processes; an example is responding to the receptor-ligand interaction.
Proteins Move Between Compartments
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Nearly all proteins are synthesized on ribosomes in the cytosol.
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Protein sorting signals (in the amino acid sequence) direct proteins to their final location.
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Four main ways proteins move between compartments: protein translocation, gated transport, vesicular transport, engulfment.
Protein Translocation
- Transmembrane proteins cross the membrane directly.
- Transmembrane protein molecule must unfold to snake through the translocator.
- Translocation into the ER lumen, ER membrane, or mitochondria occurs in this way.
Gated Transport
- Proteins and RNA molecules move between the cytosol and nucleus.
- Nuclear pore complexes act as selective gates for macromolecule transportation.
Vesicular Transport
- Membrane-enclosed transport intermediates, vesicles, or fragments of organelles transfer proteins between compartments.
- Transport intermediates are loaded with molecules from the beginning compartment.
- The contents are released at the destination compartment that it fuses with.
Endocytosis/Envelopment
- Sheets (similar to vesicles) enclose parts of the cytoplasm to form a compartment.
Sorting Signals and Receptors
- Sorting signals are amino acids in a protein (linear or three-dimensional arrangement).
- Sorting signals direct proteins to the correct cellular location.
- Signal sequences usually are at the N terminus, and they often are removed by enzymes.
Signal Sequence Specificity
- Each signal sequence directs a protein to a particular cellular destination.
- The sequences have specific characteristics distinguishing them. (positively charged, hydrophobic amino acids).
Transmembrane Protein Insertion
- Transmembrane segments are recognized by SRP and Sec61.
- Segments insert into lateral gate of Sec61 in particular orientations based on their characteristics.
Multipass Transmembrane Proteins
- Multipass proteins comprise multiple transmembrane segments.
- Orientation of each transmembrane segment depends on the adjacent segments and flanking regions.
Post-translational Translocation
- Some proteins are completely synthesized completely prior to import into the ER.
- Protein molecules are recognized by a pre-targeting complex.
- Protein is transported by cycles of BiP binding and release.
Covalently Attached GPI Anchor
- Some proteins acquire a covalently attached GPI anchor.
- A hydrophobic segment near the C-terminus is recognized and cleaved.
- The GPI anchor is attached to the rest of the protein.
Translocation Polypeptide Chains Folding-ER Lumen
- Proteins enter ER lumen as unfolded polypeptides and must fold and assemble.
- ER lumen contains high chaperone concentration to assist folding.
Oxidized Protein PDI
- Protein disulfide isomerase (PDI) catalyzes disulfide bond formation in proteins.
- This ensures correctness in protein folding in a harsh environment.
Proteins Synthesized in the Rough ER Are Glycosylated
- Oligosaccharides are often added to proteins, primarily N-linked.
- Oligosaccharides are attached at the asparagine side chains.
- Precursor oligosaccharides are synthesized on membrane-bound dolichol or a lipid.
- Oligosaccharides are flipped to the lumenal side of the ER.
- They are modified in the Golgi.
###Oligosaccharides as Protein Folding Tags
- Chaperone proteins (calnexin and calreticulin) recognize and bind oligosaccharides on incompletely folded proteins.
- Prevents aggregation and promotes correct folding.
- Glucose addition-removal cycle helps in determining proper folding.
Improperly Folded Proteins Exported
- Misfolded proteins are exported from the ER to the cytosol
- Chaperones help prevent aggregation and maintain unfolded conformation.
- E3 ubiquitin ligase marks for degradation
Misfolded Proteins in the ER Activate Protein Response
- Accumulation of misfolded proteins initiates ER unfolded protein response (UPR).
- UPR modulates transcription processes in the nucleus.
ER Assembles Most Lipid Bilayers
- The ER synthesizes nearly all major lipid classes for membranes.
- Includes phospholipids, cholesterol and ceramides.
- Phospholipid synthesis occurs in the cytosol.
- Phospholipids can move between leaflets through scramblases.
Membrane Protein Contacts
- ER and other organelles have contact sites for selective lipid transfer and protein transport.
- Specialized lipid and protein channels allow for passage between compartments.
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Description
This quiz explores the crucial functions of transport vesicles in eukaryotic cells. Understand their role in intracellular transport and how they contribute to cellular organization and function. Test your knowledge on the mechanisms and processes involving these essential cellular components.