Essential Cell Biology 5th edition
568 CHAPTER 16 Cell SignalingFigure 16–42 The ethylene signalingpathway turns on genes by relievinginhibition. (A) In the absence of ethylene,the receptor directly activates an associatedprotein kinase, which then indirectlypromotes the destruction of the transcriptionregulator that switches on ethyleneresponsivegenes. As a result, the genesremain turned off. (B) In the presenceof ethylene, the receptor and kinaseare both inactive, and the transcriptionregulator remains intact and stimulates thetranscription of the ethylene-responsivegenes. The kinase that ethylene receptorsinteract with is a serine/threonine kinase thatis closely related to the MAP kinase kinasekinase found in animal cells (see Figure16–31). Note that the ethylene receptoris located in the endoplasmic reticulum;because ethylene is hydrophobic, it passeseasily into the cell interior to reach itsreceptor.(A) ABSENCE OF ETHYLENEER LUMENCYTOSOLtranscriptionregulatoractive ethylenereceptorER membraneactiveproteinkinaseDEGRADATION(B) PRESENCE OF ETHYLENEinactiveethylenereceptorethyleneactive transcriptionregulatorinactiveproteinkinaseETHYLENE-RESPONSIVEGENES OFFTRANSCRIPTION OF ETHYLENE-RESPONSIVE GENES16−6, Movie 16.8, and Movie 16.9). This integration is made possibleby connections and interactions that occur between different signalingpathways. Such cross-talk allows the cell to bring together multiplestreams of information and react to a rich combination of signals.The most extensive links among the pathways are mediated by the proteinkinases present in each. These kinases often phosphorylate, andhence regulate, components in other signaling pathways, in addition tocomponents in their own ECB5 pathway e16.42/16.42 (see Figure 16−35). To give an ideaof the scale of the complexity, genome sequencing studies suggest thatabout 2% of our ~19,000 protein-coding genes code for protein kinases;moreover, hundreds of distinct types of protein kinases are thought to bepresent in a single mammalian cell.Many intracellular signaling proteins have several potential phosphorylationsites, each of which can be phosphorylated by a different proteinkinase. These proteins can thus act as integrating devices. Informationreceived from different intracellular signaling pathways can converge onsuch proteins, which then convert a multicomponent input to a singleoutgoing signal (Figure 16–43, and see Figure 16–9). These integratingproteins, in turn, can deliver a signal to many downstream targets. In thisway, the intracellular signaling system may act like a network of nervecells in the brain—or like a collection of microprocessors in a computer—interpreting complex information and generating complex responses.Our understanding of these intricate networks is still evolving: we are stilldiscovering new links in the chains, new signaling partners, new connections,and even new pathways. Unraveling the intracellular signalingpathways—in both animals and plants—is one of the most active areasof research in cell biology, and new discoveries are being made everyday. Genome sequencing projects continue to provide long lists of componentsinvolved in signal transduction in a large variety of organisms.Yet even if we could identify every single component in this elaborate
Essential Concepts569signal Aplasmamembranekinase 1signal Bsignal Ckinase 2PPtarget proteinCELL RESPONSEsignal DEXTRACELLULARSPACECYTOSOLFigure 16–43 Intracellular signalingproteins serve to integrate incomingsignals. Extracellular signals A, B, C, and Dactivate different receptors in the plasmamembrane. The receptors act upon twoprotein kinases, which they either activate(black arrow) or inhibit (red crossbar). Thekinases phosphorylate the same targetprotein and, when it is fully phosphorylated,this target protein triggers a cell response.It can be seen that signal molecule Bactivates both protein kinases and thereforeproduces a strong output response. SignalsA and D each activate a different kinase andtherefore produce a response only if theyare simultaneously present. Signal moleculeC inhibits the cell response and willcompete with the other signal molecules.The net outcome will depend both on thenumbers of signaling molecules and thestrengths of their connections. In a real cell,these parameters would be determined byevolution.network of signaling pathways, it will remain a major challenge to figureout exactly how they all work together to allow cells—and organisms—toECB5 e16.43/16.43integrate the diverse array of information that inundates them constantlyand to respond in a way that enhances their ability to adapt and survive.ESSENTIAL CONCEPTS• Cells in multicellular organisms communicate through a huge varietyof extracellular chemical signals.• In animals, hormones are carried in the blood to distant target cells,but most other extracellular signal molecules act over only a shortdistance. Neighboring cells often communicate through direct cell–cell contact.• For an extracellular signal molecule to influence a target cell it mustinteract with a receptor protein on or in the target cell. Each receptorprotein recognizes a particular signal molecule.• Most extracellular signal molecules bind to cell-surface receptorproteins that convert (transduce) the extracellular signal into differentintracellular signals, which are usually organized into signalingpathways.• There are three main classes of cell-surface receptors: (1) ionchannel-coupledreceptors, (2) G-protein-coupled receptors (GPCRs),and (3) enzyme-coupled receptors.• GPCRs and enzyme-coupled receptors respond to extracellular signalsby activating one or more intracellular signaling pathways,which, in turn, activate effector proteins that alter the behavior ofthe cell.• Turning off signaling pathways is as important as turning them on.Each activated component in a signaling pathway must be subsequentlyinactivated or removed for the pathway to function again.• GPCRs activate trimeric GTP-binding proteins called G proteins; theseact as molecular switches, transmitting the signal onward for a shortperiod before switching themselves off by hydrolyzing their boundGTP to GDP.• G proteins directly regulate ion channels or enzymes in the plasmamembrane. Some directly activate (or inactivate) the enzyme adenylyl
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568 CHAPTER 16 Cell Signaling
Figure 16–42 The ethylene signaling
pathway turns on genes by relieving
inhibition. (A) In the absence of ethylene,
the receptor directly activates an associated
protein kinase, which then indirectly
promotes the destruction of the transcription
regulator that switches on ethyleneresponsive
genes. As a result, the genes
remain turned off. (B) In the presence
of ethylene, the receptor and kinase
are both inactive, and the transcription
regulator remains intact and stimulates the
transcription of the ethylene-responsive
genes. The kinase that ethylene receptors
interact with is a serine/threonine kinase that
is closely related to the MAP kinase kinase
kinase found in animal cells (see Figure
16–31). Note that the ethylene receptor
is located in the endoplasmic reticulum;
because ethylene is hydrophobic, it passes
easily into the cell interior to reach its
receptor.
(A) ABSENCE OF ETHYLENE
ER LUMEN
CYTOSOL
transcription
regulator
active ethylene
receptor
ER membrane
active
protein
kinase
DEGRADATION
(B) PRESENCE OF ETHYLENE
inactive
ethylene
receptor
ethylene
active transcription
regulator
inactive
protein
kinase
ETHYLENE-RESPONSIVE
GENES OFF
TRANSCRIPTION OF ETHYLENE-
RESPONSIVE GENES
16−6, Movie 16.8, and Movie 16.9). This integration is made possible
by connections and interactions that occur between different signaling
pathways. Such cross-talk allows the cell to bring together multiple
streams of information and react to a rich combination of signals.
The most extensive links among the pathways are mediated by the protein
kinases present in each. These kinases often phosphorylate, and
hence regulate, components in other signaling pathways, in addition to
components in their own ECB5 pathway e16.42/16.42 (see Figure 16−35). To give an idea
of the scale of the complexity, genome sequencing studies suggest that
about 2% of our ~19,000 protein-coding genes code for protein kinases;
moreover, hundreds of distinct types of protein kinases are thought to be
present in a single mammalian cell.
Many intracellular signaling proteins have several potential phosphorylation
sites, each of which can be phosphorylated by a different protein
kinase. These proteins can thus act as integrating devices. Information
received from different intracellular signaling pathways can converge on
such proteins, which then convert a multicomponent input to a single
outgoing signal (Figure 16–43, and see Figure 16–9). These integrating
proteins, in turn, can deliver a signal to many downstream targets. In this
way, the intracellular signaling system may act like a network of nerve
cells in the brain—or like a collection of microprocessors in a computer—
interpreting complex information and generating complex responses.
Our understanding of these intricate networks is still evolving: we are still
discovering new links in the chains, new signaling partners, new connections,
and even new pathways. Unraveling the intracellular signaling
pathways—in both animals and plants—is one of the most active areas
of research in cell biology, and new discoveries are being made every
day. Genome sequencing projects continue to provide long lists of components
involved in signal transduction in a large variety of organisms.
Yet even if we could identify every single component in this elaborate