Podcast
Questions and Answers
Match the following cell organelles with their primary functions:
Match the following cell organelles with their primary functions:
Lysosomes = Degradation of waste materials and cellular debris Endosomes = Transport and sorting of endocytosed material Rough ER = Protein synthesis and translocation Smooth ER = Lipid synthesis and calcium storage
Match the types of ribosomes with their roles:
Match the types of ribosomes with their roles:
Membrane-bound ribosomes = Synthesize proteins for secretion or membrane localization Free ribosomes = Synthesize cytosolic and nuclear proteins Polyribosomes = Multiple ribosomes translating a single mRNA Ribosomal subunits = Combine to form functional ribosomes during translation
Match the following transport vesicle mechanisms with their descriptions:
Match the following transport vesicle mechanisms with their descriptions:
Exocytosis = Process of releasing materials outside of the cell Endocytosis = Process of internalizing substances into the cell Vesicular transport = Delivery of proteins and lipids between organelles Microtubule transport = Movement of vesicles along cytoskeletal filaments
Match the endoplasmic reticulum types with their characteristics:
Match the endoplasmic reticulum types with their characteristics:
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Match the cellular communication pathways with their functions:
Match the cellular communication pathways with their functions:
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Match the following types of ribosomes with their roles:
Match the following types of ribosomes with their roles:
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Match the following components of vesicular transport mechanisms:
Match the following components of vesicular transport mechanisms:
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Match the following cellular communication pathways:
Match the following cellular communication pathways:
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Match the following types of endocytic organelles with their characteristics:
Match the following types of endocytic organelles with their characteristics:
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Match the following endoplasmic reticulum (ER) types with their functions:
Match the following endoplasmic reticulum (ER) types with their functions:
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Match the following terms related to vesicular traffic with their definitions:
Match the following terms related to vesicular traffic with their definitions:
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Match the following cellular components with their associated functions:
Match the following cellular components with their associated functions:
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Match the following mechanisms with their descriptions:
Match the following mechanisms with their descriptions:
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Match the following functions with the corresponding type of endoplasmic reticulum:
Match the following functions with the corresponding type of endoplasmic reticulum:
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Match the following types of ribosomes with their locations:
Match the following types of ribosomes with their locations:
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Match the following pathways with their roles in cellular communication:
Match the following pathways with their roles in cellular communication:
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Match the following cellular structures with their descriptions:
Match the following cellular structures with their descriptions:
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Match the processes with their relevance to eukaryotic cell evolution:
Match the processes with their relevance to eukaryotic cell evolution:
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Match the following components of cellular structure with their functions:
Match the following components of cellular structure with their functions:
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Study Notes
Intracellular Organization and Protein Sorting
- Cellular activities and macromolecules are spatially organized in different regions within a cell.
- Eukaryotic cells, unlike bacteria, are compartmentalized into membrane-enclosed compartments for specific functions.
- These compartments are called organelles.
- Examples of organelles include the endoplasmic reticulum, Golgi apparatus, lysosomes, plastids, and mitochondria.
- Some organelles are further compartmentalized by internal membranes.
- Biomolecular condensates, dynamic assemblies of macromolecules, can act as specialized biochemical factories or temporary storage depots.
- The nucleolus is a biomolecular condensate that is not enclosed by a membrane.
Compartmentalization of Cells
- Intracellular membrane systems create enclosed compartments for biochemical reactions.
- These compartments are separate from the cytosol and create specialized aqueous spaces.
- Specialized spaces concentrate specific molecules (proteins, reactants, ions) to optimize reactions.
- Multiple compartments allow reactions needing varying conditions to occur simultaneously without interference.
Relative Volumes of Intracellular Compartments
- Cytosol accounts for 54% of a liver cell's volume.
- Mitochondria occupy 22%.
- Rough ER and smooth ER are 9% and 5% respectively.
- Golgi cisternae account for 6%.
- The nucleus takes up 1% of the cell's volume.
- Peroxisomes are 1%
- Lysosomes are 1%
- Endosomes are 1%.
Relative Amounts of Membrane Types in Eukaryotic Cells
- Liver hepatocytes have varying percentages in membrane types.
- Pancreatic exocrine cells also show different percentages in membrane type.
- Endoplasmic reticulum membrane area drastically larger (25 times in liver and 12 times in pancreatic cells) than the plasma membrane.
Evolutionary Origins of Organelles
- Eukaryotic cells arose from the merging of an anaerobic archaeon with an aerobic bacterium (1.6 billion years ago).
- Membrane expansion through protrusions likely stabilized the structure of the membrane and facilitated metabolite exchange.
- The fusion of protrusions resulted in internal compartments, including the nucleus and mitochondria.
Topological Relationships of Organelles
- The lumen of internal compartments is topologically equivalent to the extracellular space.
- The membrane-enclosed endosymbiont evolved into mitochondria.
- The common origin of organelles explains how organelles can exchange material.
- The nucleus was the cytosol in ancient archaebacteria which explains its similar topological relationship to the cytosol in eukaryotes. This similar topological arrangement allows the exchange of materials during mitosis.
Topologically Equivalent Pathways
- Molecules can be transported between topologically equivalent compartments by transport vesicles that bud from one compartment and fuse with another.
- This enables communication between various organelles and the cell exterior.
Major Intracellular Compartments
- The three main categories of compartments are the nucleus and cytosol, secretory and endocytic pathways organelles (ER, Golgi, endosomes, lysosomes), and endosymbiont-derived organelles (mitochondria, plastids).
Macromolecules Can Be Segregated Without a Membrane
- Proteins, nucleic acids, or combinations of both can form biomolecular condensates.
- These macromolecules interact through weak, fluctuating binding interactions.
- The high concentration of binding sites in local areas within the condensate helps to retain client proteins within the condensate.
- This process creates structures that can exclude the surrounding macromolecules.
Examples of Eukaryotic Biomolecular Condensates
- Condensation may be connected to functions such as ribosome assembly (nucleolus), RNA processing (Cajal body), or gene regulation (paraspeckles).
Nucleolus
- The largest and most conspicuous condensate in eukaryotic cells.
- Involved in ribosome assembly.
- Contains pre-rRNA that actively transcribes various ribosomal proteins and small nucleolar RNAs.
Biomolecular Condensates Create Biochemical Factories
- Condensates can create the necessary environment for biochemical processes to take place.
- Examples include the pyrenoid in photosynthetic bacteria, where enzymes for carbon fixation, such as Rubisco, are concentrated.
Biomolecular Condensates Form and Disassemble in Response to Need
- The formation and stability of condensates rely on weak interactions.
- Small changes in the strength of these interactions can influence the formation and properties of the condensate.
Proteins Can Move Between Compartments in Different Ways
- Proteins are synthesized on ribosomes in the cytosol.
- Amino acid sequences (sorting signals) direct proteins to correct locations in the cell.
- Four ways of protein transport include protein translocation, gated transport, vesicular transport, and engulfment.
Protein Translocation
- Transmembrane proteins are directly transported through protein translocators into the ER lumen, ER membrane, or mitochondria.
- The transported protein molecule typically needs to unfold to pass through the translocator.
Gated Transport
- Proteins and RNA molecules move between the cytosol and the nucleus through nuclear pore complexes.
- These complexes are selective gates for the active transport of molecules.
Vesicular Transport
- Membrane-enclosed vesicles move proteins from one compartment to another.
- Vesicles bud from one compartment and fuse with another to discharge their cargo.
Endocytosis
- In this process, cells engulf material from their surroundings.
- The process is similar to the formation of the nuclear envelope after mitosis.
Sorting Signals and Sorting Receptors Direct Proteins to the Correct Cell Address
- Sorting signals, composed of specific amino acid sequences, direct proteins to their correct destinations.
- These signals include linear sequences and specific three-dimensional arrangements.
- Sorting receptors recognize these signals to ensure appropriate protein transport.
Proteins with Specific Signal Sequences
- Signal sequences direct proteins to specific destinations.
- Examples of signal sequences have been provided for different protein destinations.
A Signal-Recognition Particle (SRP) Directs the ER Signal Sequence to a Specific Receptor
- The signal sequence is guided to the ER membrane by SRP and SRP receptor.
- SRP binds to the signal sequence, causing a conformational change that exposes a binding site for the SRP receptor.
- These interactions facilitate protein transport to the ER.
Membrane-Bound Ribosomes
- Ribosomes are engaged in protein synthesis and translocation across the ER membrane.
- Free ribosomes synthesize proteins that remain in the cytosol.
The Polypeptide Chain Passes Through a Signalling Sequence-Gated Aqueous Channel
- The Sec61 translocator has a lateral gate structure that opens only for proteins containing a signal sequence.
Translocation Across the ER Membrane Does Not Always Require Ongoing Polypeptide Chain Elongation
- Some proteins are completely synthesized before import.
- This type of translocation is called post-translational translocation.
Post-Translational Translocation
- This process requires additional protein complexes (Sec62, Sec63) to position BiP molecules in the ER lumen, where they bind and pull the protein into the lumen, assisted by ATP-driven cycles.
Transmembrane Proteins Contain Hydrophobic Segments That Are Recognized Like Signal Sequences
- Transmembrane proteins have hydrophobic segments to span the ER membranes.
- These segments are similar to signal sequences that direct soluble proteins into the ER.
A Transmembrane Segment Directs Membrane Protein Insertion
- Transmembrane segments direct insertion into the ER membrane.
- This process can occur with two potential orientations determined by the flanking amino acids.
Many Transmembrane Proteins Contain Large N-Terminal Lumenal Domains
- Many transmembrane proteins having N-terminal domains can use signal sequences in similar ways as soluble proteins.
- After the hydrophobic segment gets incorporated into the ER membrane, the rest of the protein is synthesized in the cytosol.
Hydrophobic Segments of Multiple-Pass Transmembrane Proteins Are Interpreted Contextually to Determine Their Orientation
- The insertion of transmembrane domains determines protein orientation in the membrane.
Some Proteins Are Integrated into the ER Membrane by a Post-Translational Mechanism
- Tail-anchored proteins are integrated into the ER membrane by a post-translational mechanism.
- A pre-targeting complex captures the hydrophobic C-terminal transmembrane segment to transport it to the ER.
Some Membrane Proteins Acquire a Covalently Attached Glycosylphosphatidylinositol (GPI) Anchor
- GPI anchors are covalently linked to the C-terminus of some proteins for transmembrane proteins' attachment.
- Proteins initially are made with an N-terminal signal sequence, a hydrophobic segment close to the C-terminus. Recognition by a transamidase enzyme, it cleaves the hydrophobic segment and attaches the anchor.
Translocated Polypeptide Chains Fold and Assemble in the Lumen of the Rough ER
- Proteins fold into correct three-dimensional structures in the ER lumen.
- Specific chaperone proteins in the ER lumen help with folding and assembly.
The ER Resident Protein Protein Disulfide Isomerase (PDI)
- PDI catalyzes the oxidation of free SH groups on cysteines to form disulfide bonds.
- Disulfide bonds help proteins maintain proper conformation.
Most Proteins Synthesized in the Rough ER Are Glycosylated
- Proteins are often glycosylated in the ER with common N-linked oligosaccharides.
- This occurs via a preformed precursor oligosaccharide that is transferred to a specific asparagine.
The Oligosaccharide in N-Linked Glycosylation
- Precursor oligosaccharide is built up on the membrane-bound dolichol lipid.
- Then transferred with the help of transporters from the cytosol to the ER lumen.
- Commonly linked to 90% of existing glycoproteins.
Oligosaccharides Are Used as Tags to Mark the State of Protein Folding
- Oligosaccharides act as tags to mark the folding state of proteins.
- Chaperones like calnexin and calreticulin bind to incompletely folded proteins that contain a terminal glucose.
- This process helps to ensure proper folding.
Improperly Folded Proteins Are Exported
- Misfolded proteins are exported from the ER to the cytosol for degradation.
- The proteins are recognized, marked with ubiquitin to prevent aggregation, and sent for disposal in the proteasomes through protein translocation mechanisms.
Misfolded Proteins in the ER Activate an Unfolded Protein Response
- An accumulation of misfolded proteins in the ER triggers the unfolded protein response. This initiates a cascade of signaling pathways that promote protein folding capacity and degradation so the cell can cope with the stress of misfolded proteins.
The ER Assembles Most Lipid Bilayers
- ER membranes are the primary site for synthesizing nearly all major lipid classes.
- Enzymes within the ER membrane synthesize phospholipids, like phosphatidylcholine, starting from simpler components.
- Further processes produce other vital lipids like phosphatidylethanolamine, phosphatidylserine, phosphatidylinositol, cholesterol and ceramide.
Membrane Contact Sites Between the ER and Other Organelles Facilitate Selective Lipid Transfer
- Selective lipid transfer happens at contact sites, not via vesicles.
- Lipid transfer proteins help move lipids between the ER and other organelles, such as mitochondria.
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Description
Test your knowledge of cell biology by matching various organelles with their functions. This quiz covers ribosomes, endoplasmic reticulum types, vesicular transport mechanisms, and cellular communication pathways. Perfect for students looking to solidify their understanding of cellular components and their roles.