Campbell Biology · Chapter 11
Cell Communication
pp. 206–227 · 5 sections
Cells are always sending and receiving messages, and this chapter follows one message from the moment it reaches a cell to the cell's reaction: reception, transduction and response. It ends with apoptosis, the planned cell death that signals can trigger. Almost all of it lines up with the first three topics of AP Unit 4, so expect to predict what happens when a receptor, relay protein or second messenger is broken or blocked.
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11.1 How cells send and receive messages
pp. 206–210
Topics 4.1 and 4.2 cover this: know contact, local and long-distance signaling and the reception, transduction and response outline. You won't need the history of who worked it out.
In the course: Topic 4.1 Cell Communication, Topic 4.2 Introduction to Signal Transduction, Topic 7.7 Common Ancestry (notes, videos and more questions)
Key points
- Every kind of cell, from a bacterium to a neuron, picks up signals and reacts to them. Most signals are chemicals, though light, touch and temperature can act as signals too.
- Bacteria use quorum sensing to judge how crowded they are. Each cell leaks a small signal molecule, and once its level climbs past a threshold, the whole group switches genes on together, for jobs like building a biofilm or glowing.
- Yeasts, plants and animals share many of the same signaling parts. That suggests the basic toolkit arose early in single-celled ancestors and was later reused by multicellular life.
- Some cells signal by touching. Gap junctions (animals) and plasmodesmata (plants) are open channels between neighboring cells. Animal cells can also recognize each other when a surface protein on one cell latches onto a partner protein on another, which is how many immune cells check each other.
- Local signals travel only a short way. Growth factors and other local regulators drift to nearby cells (paracrine signaling), and neurotransmitters cross the tiny gap of a synapse to the next cell.
- Long-distance signals are hormones. Animal hormones ride the bloodstream. Plant hormones spread through tissues and veins, and a few are gases that can even reach neighboring plants through the air. A cell responds only if it has a receptor that fits the hormone.
- Seen from the cell that gets the message, signaling happens in three steps: reception (the signal binds a receptor), transduction (the message is relayed and changed inside the cell) and response (the cell does something). Usually the signal molecule itself never gets inside.
Key terms (14)
- cell signaling
- Communication in which one cell sends a message, usually a chemical, and another cell detects it and changes what it's doing.
- target cell
- Any cell that has the right receptor for a particular signal and so can respond to it. Cells without that receptor ignore the signal.
- quorum sensing
- The way bacteria measure how many of their kind are nearby by tracking the level of a signal molecule they all release, then act as a group once the level is high enough.
- biofilm
- A slimy layer of microbes stuck to a surface and to each other, like the film that coats the inside of water pipes. Bacteria often build one only after quorum sensing tells them their numbers are high.
- gap junction
- A channel joining two neighboring animal cells so ions and small molecules can flow straight from one cytoplasm to the other.
- plasmodesmata
- Openings through plant cell walls that link neighboring plant cells' cytoplasm, so small molecules can pass between them.
- local regulator
- A signal molecule that only reaches cells near the cell that released it, such as a neurotransmitter or a growth factor.
- paracrine signaling
- Local signaling in which a cell releases a regulator into the fluid around it and nearby cells respond.
- synaptic signaling
- Signaling in the nervous system: a neuron releases a neurotransmitter into a synapse, and it quickly reaches the next cell.
- hormone
- A signal molecule that travels a long way to reach target cells. In animals it usually travels in the blood.
- endocrine signaling
- Long-distance signaling in animals in which gland cells release hormones into the blood or other body fluids, which carry them to distant targets.
- reception
- The first stage of signaling: the target cell detects the signal when it binds a matching receptor protein.
- transduction
- The middle stage of signaling: the message is passed along inside the cell and turned into a form that can cause a response.
- cellular response
- The last stage of signaling: what the cell actually does, such as switching on a gene, changing an enzyme's activity or dividing.
Check yourself: 11.1 How cells send and receive messages
4 questions on 11.1 How cells send and receive messages. Pick an answer to see if you got it, and why.
After a minor cut, platelets at the wound release a protein that spreads only a short distance through the tissue fluid and stimulates nearby skin cells to divide. Which type of signaling does this describe?
A marine bacterium releases a small signal molecule and makes a light-producing enzyme. Researchers grow cultures at different densities and measure both (invented data). Cell density (cells/mL) | Signal molecule in medium (nM) | Light output (relative units) 10⁶ | 2 | 1 10⁷ | 20 | 2 10⁸ | 200 | 950 10⁹ | 2,000 | 1,000 Which conclusion is best supported by the data?
Cell population A triggers a response in cell population B when the two are grown mixed together. Researchers then grow them in the same dish separated by a porous filter that lets dissolved molecules and proteins pass but keeps the cells from touching. Population B no longer responds. What is the most reasonable conclusion?
A fluorescent sugar too large and polar to cross a plasma membrane is injected into a single cell of a moss leaf. Within minutes it appears in the cytoplasm of the surrounding cells. Which structures most likely allowed this?
0 of 4 answered
11.2 Reception: receptors and their signals
pp. 210–214
Topic 4.2 covers surface receptors such as G protein-coupled receptors and ligand-gated channels, plus receptors inside the cell; receptor tyrosine kinase details like pairing up are useful background.
In the course: Topic 4.2 Introduction to Signal Transduction, Topic 2.4 Membrane Permeability, Topic 4.3 Signal Transduction Pathways (notes, videos and more questions)
Key points
- A signal molecule is a ligand: it fits a specific binding site on its receptor, so a receptor ignores molecules of the wrong shape. Binding usually changes the receptor's shape, and that shape change is what starts the message moving.
- Large or water-soluble ligands, such as peptide hormones, can't get through the oily middle of the membrane. Their receptors span the plasma membrane, with the binding site outside and a working part inside.
- G protein-coupled receptors (GPCRs) are the biggest family, roughly 800 in humans, covering smell, taste, vision and many hormones. An active GPCR makes its G protein swap GDP for GTP, which switches the G protein on; it then turns on an enzyme or channel. The G protein switches itself off by splitting GTP back to GDP.
- Receptor tyrosine kinases (RTKs) pair up when the ligand binds, and each tags tyrosines on its partner's tail with phosphates. Each tagged tyrosine becomes a landing spot for a particular relay protein, which lets a single receptor launch several pathways together.
- In a ligand-gated ion channel, binding of the ligand opens (or sometimes closes) a gate, letting specific ions like Na⁺, Ca²⁺ or Cl⁻ through. They're very fast, which is why neurons rely on them.
- Small or nonpolar signals, such as steroid hormones, thyroid hormone and nitric oxide, slip through the membrane and bind receptors in the cytoplasm or nucleus. The hormone–receptor pair often works as a transcription factor, switching genes on or off.
- Faulty receptors cause disease: overactive RTKs drive some cancers, and about a third of today's medicines act on GPCRs.
Key terms (15)
- ligand
- A molecule that binds specifically to another, usually larger, molecule. A signal molecule is the ligand of its receptor.
- receptor
- A protein that recognizes one particular signal by its shape and changes when the signal binds, starting the cell's response.
- ligand-binding domain
- The part of a receptor that holds the signal molecule. A mutation here can stop the right signal from fitting.
- G protein-coupled receptor (GPCR)
- A membrane receptor made of one chain that crosses the membrane seven times. When a signal binds, it switches on a G protein inside the cell.
- G protein
- A protein on the inner face of the membrane that's off when it holds GDP and on when it holds GTP. It passes the signal from a GPCR to an enzyme or channel.
- GTP
- Guanosine triphosphate, a nucleotide with three phosphates that's a close relative of ATP. A G protein is active while GTP is bound to it.
- GTPase
- An enzyme that splits GTP to GDP. G proteins have this activity built in, so they switch themselves off.
- protein kinase
- An enzyme that moves a phosphate group from ATP onto a protein, which changes that protein's shape and activity.
- receptor tyrosine kinase (RTK)
- A membrane receptor whose inner part is a kinase. When a signal binds, two receptors pair and add phosphates to tyrosines on each other's tails.
- dimer
- A unit made of two protein subunits joined together, like two RTKs paired up after their signal binds.
- ligand-gated ion channel
- A membrane channel that opens or closes when a specific signal binds it, controlling the flow of particular ions.
- intracellular receptor
- A receptor in the cytoplasm or nucleus. Its signals can slip through the plasma membrane on their own because they're small or nonpolar.
- steroid hormone
- A lipid hormone built on a four-ring structure, like estrogen or cortisol. It crosses membranes easily and acts on receptors inside the cell.
- transcription factor
- A protein that binds DNA and helps switch particular genes on or off.
- antagonist
- A drug or molecule that binds a receptor without activating it, blocking the natural signal from binding.
Check yourself: 11.2 Reception: receptors and their signals
4 questions on 11.2 Reception: receptors and their signals. Pick an answer to see if you got it, and why.
A drug fits snugly into the ligand-binding site of a hormone receptor but does not cause the shape change that the hormone causes. What is the most likely effect of giving the drug along with the hormone?
A mutant G protein binds to its activated receptor normally but cannot release GDP, so it never picks up GTP. Which outcome is most likely when the receptor's ligand is present?
In a recording from a muscle cell, ions begin flowing across the plasma membrane less than a millisecond after a signal molecule arrives. The response needs no ATP, no enzyme activity and no second messenger inside the cell. Which kind of receptor most likely detects this signal?
In a receptor tyrosine kinase, researchers replace every tyrosine on the receptor's intracellular tail with phenylalanine, an amino acid that cannot be phosphorylated. The ligand-binding domain is unchanged. When the ligand is added, which result is most likely?
0 of 4 answered
11.3 Transduction: relays, kinases and second messengers
pp. 214–219
Topic 4.2 expects phosphorylation cascades and second messengers such as cAMP. IP₃, DAG and phospholipase C are background, and you won't need their names.
In the course: Topic 4.2 Introduction to Signal Transduction, Topic 4.3 Signal Transduction Pathways (notes, videos and more questions)
Key points
- Most membrane receptors start a relay of several steps inside the cell. More steps give the cell more chances to amplify the signal and to adjust it.
- The signal molecule isn't handed down the line. What travels is information, as each relay molecule changes shape and changes the next one.
- Protein kinases move a phosphate from ATP onto a protein, usually on a serine, threonine or tyrosine. That often switches the protein on, though sometimes it switches it off. In a phosphorylation cascade, one kinase activates the next, which activates the next.
- Protein phosphatases strip the phosphates off again. Kinases and phosphatases pull in opposite directions, so a protein's activity reflects which side is winning at that moment, and phosphatases reset the pathway once the signal is gone.
- Second messengers are small, nonprotein molecules or ions that spread quickly through the cytosol. Adenylyl cyclase, which a G protein can switch on, turns ATP into cyclic AMP (cAMP). cAMP usually activates protein kinase A, and phosphodiesterase breaks cAMP down to end the signal.
- Calcium ions are an even more common second messenger. Pumps keep cytosolic Ca²⁺ thousands of times lower than outside the cell or inside the ER, so opening Ca²⁺ channels for a moment makes the level jump.
- In one common route, an enzyme splits a membrane phospholipid into two messengers, IP₃ and DAG. IP₃ opens Ca²⁺ channels in the ER, releasing calcium into the cytosol.
Key terms (13)
- signal transduction pathway
- The chain of steps inside a cell that links a signal binding its receptor to the cell's response.
- relay molecule
- Any molecule in a signaling pathway that receives the message from the step before it and passes it on.
- phosphorylation
- Adding a phosphate group to a molecule. On a protein it changes the shape, which usually turns the protein on or off.
- phosphorylation cascade
- A chain of kinases in which each one phosphorylates and activates the next, passing the signal down the line.
- protein phosphatase
- An enzyme that removes phosphate groups from proteins, undoing what kinases did and helping shut a pathway off.
- second messenger
- A small, nonprotein molecule or ion, such as cAMP or Ca²⁺, that spreads a signal through the cell after the first messenger binds outside.
- cyclic AMP (cAMP)
- A small ring-shaped molecule made from ATP that carries signals inside the cell, often by switching on protein kinase A.
- adenylyl cyclase
- A membrane enzyme that turns ATP into cAMP. In many pathways an active G protein switches it on.
- phosphodiesterase
- The enzyme that breaks cAMP down into plain AMP, which ends the cAMP signal once the outside signal stops.
- protein kinase A
- A kinase that cAMP switches on. It then phosphorylates other proteins, which differ from one kind of cell to another.
- calcium ion (Ca²⁺)
- A widely used second messenger. The cytosol keeps very little of it, so a burst of Ca²⁺ is easy for the cell to notice.
- IP₃ (inositol trisphosphate)
- A small second messenger cut from a membrane phospholipid. It opens calcium channels in the ER membrane.
- DAG (diacylglycerol)
- The part of the split phospholipid that stays in the membrane after IP₃ is released, where it acts as a second messenger too.
Check yourself: 11.3 Transduction: relays, kinases and second messengers
4 questions on 11.3 Transduction: relays, kinases and second messengers. Pick an answer to see if you got it, and why.
Which property of second messengers such as Ca²⁺ and cAMP best explains why they can spread a signal through the cytosol faster than most relay proteins can?
A pathway contains three kinases, K1, K2 and K3. Researchers delete each kinase in turn, add the signal, and check which kinases become phosphorylated (invented data). Cell line | K1 phosphorylated? | K2 phosphorylated? | K3 phosphorylated? | Response? Normal | Yes | Yes | Yes | Yes K1 deleted | — | No | No | No K2 deleted | Yes | — | No | No K3 deleted | Yes | Yes | — | No What order of the kinases in the cascade do the data support?
In one pathway, the final target enzyme is switched OFF when a kinase phosphorylates it, and a phosphatase switches it back on. What would most likely happen to this enzyme's activity if the cell were treated with a drug that blocks the phosphatase?
In a resting animal cell, the cytosolic Ca²⁺ concentration is 100 nM (1.0 × 10⁻⁷ M), and the concentration in the surrounding fluid is 1.2 mM (1.2 × 10⁻³ M). Which choice gives the correct ratio and explains why Ca²⁺ works well as a second messenger?
0 of 4 answered
11.4 Responses: what the cell does, and how it's controlled
pp. 219–223
Topics 4.2 and 4.3 cover amplification, the kinds of responses and predicting what a blocked or stuck step does; scaffolding proteins and cross-talk are background.
In the course: Topic 4.2 Introduction to Signal Transduction, Topic 4.3 Signal Transduction Pathways, Topic 6.6 Gene Expression and Cell Specialization (notes, videos and more questions)
Key points
- A nuclear response changes gene expression: the last relay molecule activates a transcription factor that switches genes on or off, so new proteins are made. It takes minutes to hours.
- A cytoplasmic response changes proteins the cell already has, such as opening a channel, switching on an enzyme or rebuilding the cytoskeleton to change shape or move. It can happen in seconds.
- Signals are amplified. Each active enzyme in a pathway acts on many molecules of the next one, so a handful of ligand molecules outside can change millions of molecules inside.
- Which cells respond, and how, comes down to the proteins each cell type makes. Gene expression decides a cell's receptors and its relay and response machinery, so one signal can make one cell type contract, another secrete, and a third ignore it.
- Pathways branch and connect. One signal can start several responses, and two signals can feed into one response. Scaffolding proteins keep groups of relay proteins side by side, so the message doesn't depend on proteins drifting into each other by chance.
- To respond again, a cell has to reset. Phosphatases strip phosphates off relay proteins, phosphodiesterase clears away cAMP, each G protein turns itself off by splitting its GTP, and receptors empty out as the outside signal fades.
Key terms (10)
- nuclear response
- A signaling outcome in which genes are switched on or off, changing which proteins the cell makes.
- cytoplasmic response
- A signaling outcome that changes the activity of proteins already in the cell, like enzymes, channels or the cytoskeleton.
- signal amplification
- The way a signal grows stronger as it moves down a pathway, because each active enzyme acts on many molecules of the next step.
- specificity
- The fact that a signal affects only cells with the right receptor, and that different cells can respond to it in different ways.
- branching
- When one signal splits into several pathways inside a cell, producing more than one response at once.
- cross-talk
- Interaction between different signaling pathways, so one pathway can boost, block or change another's effect.
- scaffolding protein
- A protein that acts as a docking platform, keeping several relay proteins of one pathway side by side so the message passes quickly.
- signal termination
- Switching a pathway off once the signal is gone, so the cell can reset and respond to the next signal.
- threshold
- The minimum level of signal, or of active receptors, needed before a cell responds at all.
- growth factor
- A signal molecule that tells target cells to grow and multiply. Faulty growth factor pathways can contribute to cancer.
Check yourself: 11.4 Responses: what the cell does, and how it's controlled
4 questions on 11.4 Responses: what the cell does, and how it's controlled. Pick an answer to see if you got it, and why.
In a model pathway, 3 hormone molecules each bind one receptor. Each receptor activates 40 G proteins, and each G protein switches on one enzyme. Each enzyme makes 250 second-messenger molecules, it takes 4 second-messenger molecules to activate one kinase, and each kinase activates 30 target proteins. How many target proteins are activated in total?
Two signals, A and B, each cause a response in the same cell type. Researchers measure each response with and without a drug that blocks protein synthesis (invented data). Signal | Response at 2 min, no drug | Response at 3 h, no drug | Response at 3 h, with drug A | Strong | Strong | Strong B | None | Strong | None Which conclusion is best supported?
Histamine causes smooth muscle cells in the airways to contract, but it causes certain stomach lining cells to secrete acid. Which explanation best accounts for the two different responses to the same signal?
Two versions of a signal molecule activate the same receptor. Version N binds and lets go like a normal ligand. Version X forms a permanent covalent bond with the receptor. Both are added to separate dishes of cells and then washed away. What would most likely happen after the washout?
0 of 4 answered
11.5 Apoptosis: programmed cell death
pp. 223–225
Apoptosis is a possible outcome of signaling (Topic 4.3) and of cell-cycle trouble (Topic 4.6). You won't need caspase names, the mitochondrial steps or the worm genes researchers studied.
In the course: Topic 4.3 Signal Transduction Pathways, Topic 4.6 Regulation of Cell Cycle (notes, videos and more questions)
Key points
- Apoptosis is a cell's built-in, orderly self-destruct program. As it dies, the cell shrinks, chops up its own DNA and pinches off sealed bubbles of membrane (blebs), and phagocytes then swallow the pieces.
- Because the contents stay wrapped up, apoptosis doesn't spill harmful enzymes or cause inflammation. A cell that bursts from injury, called necrosis, does spill them.
- The work is done by protein-cutting enzymes called caspases and by DNA-cutting nucleases. Cells keep these enzymes on hand in a switched-off state, so starting apoptosis means activating them, not building them from scratch, and it can begin fast.
- In mammals, a major route runs through the mitochondria: pores form in the outer membrane, and released proteins such as cytochrome c help switch caspases on. Competing groups of pro-death and pro-survival proteins decide whether that happens.
- Triggers come from outside, such as a death signal binding a surface receptor, or from inside, such as DNA damage that can't be repaired or a pile-up of misfolded proteins in the ER. The cell weighs survival signals against death signals.
- Apoptosis shapes the body, for example clearing out a tadpole's tail as it becomes a frog and trimming extra neurons, and it clears infected, damaged or unneeded cells. Too little can contribute to cancer, and too much to diseases that destroy neurons.
- Apoptosis genes are similar in worms, flies and mammals, and apoptosis-like death has been reported even in yeasts, so the basic program probably evolved early in eukaryotes.
Key terms (10)
- apoptosis
- A controlled form of cell death in which a cell takes itself apart in an orderly way without harming its neighbors.
- programmed cell death
- Cell death carried out by the cell's own genetic program, rather than caused by injury. Apoptosis is the most studied form.
- necrosis
- Unplanned cell death from injury, in which the cell swells and bursts and its contents spill out and trigger inflammation.
- caspase
- One of a family of protein-cutting enzymes that do most of the demolition in apoptosis. They wait in the cell in an inactive form until switched on.
- nuclease
- An enzyme that cuts DNA or RNA. During apoptosis, nucleases chop the cell's DNA into fragments.
- blebbing
- The bulging and pinching off of the membrane of a dying cell into small sealed pieces.
- phagocyte
- A cell that engulfs and digests other cells or debris, including the remains of cells that died by apoptosis.
- cytochrome c
- A protein that normally carries electrons in mitochondria. When it leaks into the cytosol, it helps switch on apoptosis.
- death signal
- A molecule or internal alarm, such as severe DNA damage, that pushes a cell toward apoptosis.
- survival factor
- A signal from other cells that tells a cell to stay alive. Losing it can push the cell toward apoptosis.
Check yourself: 11.5 Apoptosis: programmed cell death
4 questions on 11.5 Apoptosis: programmed cell death. Pick an answer to see if you got it, and why.
A virus-infected cell in the lining of the lungs dies by apoptosis rather than bursting. Which feature of apoptosis best protects the surrounding healthy tissue?
Cultured cells are treated with a drug that completely blocks protein synthesis. When a death signal is added 10 minutes later, the cells still undergo apoptosis on the normal schedule. What best explains this result?
Normal cells and mutant cells lacking a protein that detects DNA damage are exposed to the same dose of radiation. After 24 hours, 45% of the normal cells but only 4% of the mutant cells have undergone apoptosis, and the mutant survivors carry many unrepaired DNA breaks. Which long-term risk is greatest for tissue made of the mutant cells?
A drug prevents pores from forming in the outer mitochondrial membrane, so mitochondria cannot release proteins that promote cell death. Which trigger could most likely still cause apoptosis in cells treated with this drug?
0 of 4 answered