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Growth factor Dimerized receptor
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The SH2 DOMAIN links an activated (autophosphorylated) receptor to various downstream pathways Each of the proteins has a common SH2 adaptor domain fused to another domain that performs the downstream function The same signal can then activate multiple pathways GNRP and GAP represent adaptors that can affect G-protein signaling (see the following section G-Protein Coupled Receptors )
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G-PROTEIN COUPLED RECEPTORS
These activate a G-protein that activates downstream signals G-proteins are molecular timers G-protein activation usually leads to an increase in second messenger concentrations (Ca2 or cAMP) GTPase activating protein (GAP) inactivates the G-protein by increasing GTPase activity Guanine nucleotide exchange factors (GNEF) activate the G-protein by increasing the rate of exchange of GDP for GTP G-proteins are molecular timers that couple transmembrane receptor activation to downstream members of the pathway (Fig 9-5) They are called G-proteins because they are intimately involved with the nucleotide, GTP Before activation, the G-protein is hanging around in its GDP form When the activated receptor finds its G-protein it activates it by increasing the rate of exchange between GTP and GDP Once activated, the G-protein interacts with downstream effectors and can activate
Growth factor
GNRP
Ras GTP
Inactivated Ras
Activated Ras
Ras GAP
Figure 9-5 G-protein Coupled Receptors
The Ras pathway is shown here Ras is a G-protein that couples signaling from growth factors The activated receptor is a GNRP that increases the exchange of GDP for GTP and activates the G-protein Ras GAP inactivates the G-protein The downstream signal for activated Ras is eventually the mitogen-activated protein kinase pathway (MAPK)
Basic Concepts in Biochemistry
them or inhibit them (depending on what needs to be done) G-proteins have an intrinsic enzyme activity that hydrolyzes the GTP This is the timer When the timer runs down (GTP is hydrolyzed to GDP), the signal goes away and the signaling is stopped There are two ways to affect the timing of G-proteins Affector proteins can interact with the GDP form of the G-protein and make the release of GDP and the binding of GTP faster These proteins are called guanine nucleotide exchange factors (GNEF), or guanine nucleotide release proteins (GNRP), depending on who is using the name (rather than any functional difference) Their effect is to help activate the signaling pathway Other signaling molecules in the pathway can activate the GTPase activity They make the G-protein inactivate faster (speed up the clock) and inactivate the signaling pathway These are called GAPs (GTPase-activating proteins) Most G proteins activate events that lead to an increase in second messenger concentrations (Ca2 or cAMP); we ll talk about that later There are different kinds of G-proteins The trimeric G-proteins are used mainly with transmembrane receptors They have three subunits, , , and The subunit is the GTPase part, but it s kept in its GDP form when it is bound to the - subunits When GTP is bound, the -subunit is released as an activated G-protein The activated G-proteins can stimulate some downstream enzyme (these are called stimulatory G-proteins, or Gs) However, some G-proteins may be inhibitory in their active form they re called Gi Whether the target protein is stimulated or inhibited will depend on the type of G-protein There are also monomeric G-proteins Just like the trimeric G-proteins, they are involved as signal relays and timers The Ras superfamily relays signals from receptor tyrosine kinases to downstream elements that eventually regulate transcription Rho and Rac relay signals from cellsurface receptors to the cytoskeleton, while Rab regulates intracellular transport of vesicles Regardless of what they do, they use the timer mechanism provided by the G-protein Three-letter acronyms (TLA), such as Ras, Rho, and Rab, are difficult to remember, sometimes even when you know what the letters stand for Unfortunately, there s nothing you can do about this except to memorize them
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