Download CPPS 325 FINAL EXAM with correct answers and more Exams Biology in PDF only on Docsity!
CPPS |\ 325 |\FINAL |\EXAM |\with |\correct |\answers
What |\are |\the |\ 5 |\well-known |\enzyme-linked |\cell |\surface |\receptors? |- |\CORRECT |\ANSWERS |\✔✔1. |\Receptor |\Guanylyl |\Cyclase: |\produces |\cGMP
- |\RTK: |\phosphorylate |\tyrosine |\residues |\leading |\to |\association |\of |
signalling |\molecules |\and |\cascade - |\TK |\Associated |\Receptors: |\associate |\with |\proteins |\having |\TK |
activity |\ - |\Receptor |\Tyrosine |\Phosphates: |\Removes |\phosphate |\on |\tyrosine |\residues |\
- |\Receptor |\Serine/Threonine |\Kinases: |\phosphorylate |\specific |
Serine/Threonine |\residues |\on |\IC |\signalling |\molecules How |\are |\RTK |\and |\TK |\Associated |\Receptors |\different? |- |\CORRECT |
ANSWERS |\✔✔RTK |\phosphorylate |\tyrosine |\while |\associated |
receptors |\bind/find |\proteins |\with |\TK |\activity |\to |\initiate |\the |
cascade |\of |\signalling. What |\is |\the |\reciprocal |\of |\RTK? |- |\CORRECT |\ANSWERS |\✔✔Receptor |
Tyrosine |\Phosphatases. |\They |\take |\the |\phosphate |\off |\the |\tyrosine |
residues |\to |\inactivate |\signalling |\cascades. |
Ex. |\Transforming |\GF |\Beta |\superfamily |\of |\receptors, |\cell |\type |
dependent. What |\is |\the |\major |\mechanism |\for |\receptor |\signal |\transduction? |- |
CORRECT |\ANSWERS |\✔✔Tyrosine |\kinase |\phosphorylation
RTK |\vs. |\Serine/Threonine |\Phosphorylation |? |- |\CORRECT |\ANSWERS |\✔✔Tyrosine |\phosphorylation |\is |\rare |(1%) |\relative |\to |\serine/threonine |\residue |\phosphorylation. |\Tyrosine |
phosphorylation |\is |\the |\major |\mechanism |\of |\receptor |\signal |
transduction. What |\is |\the |\net |\effect |\of |\activated |\TKs? |- |\CORRECT |\ANSWERS |
✔✔Tyrosine |\phosphorylation |\on |\target |\proteins. What |\do |\TK |\pathways |\mediate? |- |\CORRECT |\ANSWERS |\✔✔Cell |
growth |(growth |\factors), |\differentiation, |\host |\defense, |\metabolic |
regulation, |\cell |\survival |\pathways |(survival |\factors). What |\are |\amplifiers |\of |\the |\TK |\pathways? |- |\CORRECT |\ANSWERS |
✔✔PI3-K |-> |\PIP3 |
PLC |-> |\DAG |\and |\InsP3&Ca2+ What |\are |\RTK |\mediated |\actions |\in |\the |\cell? |- |\CORRECT |\ANSWERS |
✔✔regulation |\of |\cell |\proliferation, |\differentiation, |\and |\cell |\motility, |\promotion |\of |\cell |\survival |\and |\modulation |\of |\cellular |\metabolism. TKs |\exist |\in |\either |\the |\cytosol |\or |\as |\transmembrane |\receptors, |
what |\are |\the |\differences |\in |\the |\two |\types? |- |\CORRECT |\ANSWERS |
✔✔Cytosol |\receptors |\have |\an |\src |\N-terminal |\region. |\Cytosol |\has |
no |\membrane |\spanning |\domain.
What |\is |\SH2 |\domain |\characterized |\by? |- |\CORRECT |\ANSWERS |
✔✔Binds |\peptides |\with |\consensus |(positional |\information |\on |\C- terminal |\side |\of |\the |\phosphorylated |\tyrosine). |
Very |\specific. |
Mediates |\protein-protein |\interactions |\in |\cellular |\signalling |
cascades. |\Very |\common |\in |\proteins |\outside |\the |\src |\family. What |\do |\SH2 |\and |\SH3 |\domains |\have |\as |\a |\common |\funciton? |- |
CORRECT |\ANSWERS |\✔✔They |\mediate |\protein-protein |\interactions |\in |\cellular |\signalling |\cascades. |
Very |\common |\in |\proteins |\outside |\the |\src |\family. What |\is |\SH3 |\domain |\characterized |\by? |- |\CORRECT |\ANSWERS |
✔✔Interacts |\with |\proline-rich |\peptide |\targets |(minimal |
consensus). |\Mediate |\protien-protein |\interatctions |\in |\the |\cellular |
signalling |\cascade. |\Very |\common |\in |\proteins |\outside |\the |\src |
family. What |\are |\PTB |\domains? |- |\CORRECT |\ANSWERS |
✔✔(Phosphotyrosine |\binding |\domain) |
Bind |\to |\phosphorylated |\tyrosine. |\Functional |\equivalent |\of |\the |\SH |\domain, |\except |\for |\the |\positional |\informational. |\Is |\not |\the |\C- terminus |\like |\SH2, |\but |\the |\N-terminus |\side |\of |\the |\phosphorylated |
tyrosine. shc |\is |\a |\PTB |\protein. What |\is |\the |\normal |\action |\that |\stops |\signalling |\for |\cell |\division |\in |
the |\src |\pathway? |- |\CORRECT |\ANSWERS |\✔✔Contact |\Inhibition |
Confluency
How |\do |\PTB |\and |\SH2 |\domains |\differ? |- |\CORRECT |\ANSWERS |
✔✔SH2 |\domains |\binds |\consensus |\on |\the |\C-terminus. PTB |\domains |\binds |\the |\N-terminus. |
They |\both |\mediate |\cellular |\signalling. What |\is |\shc? |- |\CORRECT |\ANSWERS |\✔✔PTB |\protein |\that |\docks |\at |
the |\N-terminus |\consensus |\docking |\site. What |\activates |\a |\RTK? |- |\CORRECT |\ANSWERS |\✔✔Ligand/agonist |
binding Upon |\ligand |\binding |\the |\two |\activation |\pathways |\are? |- |\CORRECT |\ANSWERS |\✔✔1. |\Conformational |\change
- |\Dimerization What |\happens |\with |\conformational |\change |\activation? |- |\CORRECT |\ANSWERS |\✔✔A |\conformational |\change |\that |\is |\sufficient |\enough |
to |\activate |\SH1/catalytic |\domain |\results |\in |\phosphorylation. What |\is |\the |\only |\example |\of |\conformational |\change |\activation? |- |
CORRECT |\ANSWERS |\✔✔Insulin |\receptor |\kinase. All |\other |\RTKs |\are |\activated |\through |\forms |\of |\dimerization. What |\are |\the |\two |\forms |\of |\dimerization? |- |\CORRECT |\ANSWERS |
✔✔i) |\Receptors |\exist |\as |\unactivated |\dimers |\until |\ligand |\binds |
(Twist |\theory)
phosphorylation |\outside |\the |\catalytic/kinase |\domain |\that |
produces |\a |\docking |\site. What |\does |\phosphorylation |\of |\tyrosines |\within |\the |\kinase/catalytic |\domain |\do? |- |\CORRECT |\ANSWERS |\✔✔Increases |
the |\kinase |\activity |\of |\the |\enzyme. What |\does |\phosphorylation |\of |\tyrosines |\outside |\the |\kinase/catalytic |\domain |\do? |- |\CORRECT |\ANSWERS |\✔✔It |\creates |
high-affinity |\binding |\sites |\for |\a |\number |\of |\IC |\signalling |\properties. What |\are |\some |\IC |\signalling |\proteins |\that |\bind |\to |\the |\docking |
sites |\created |\by |\phosphorylation |\outside |\the |\kinase/catalytic |
domain? |- |\CORRECT |\ANSWERS |\✔✔- |\PLC |(amplifiers) |\which |\leads |
to |\release |\of |\Ca2+ -SRC |\TK |(non-receptor |\TK) -Adaptor |\proteins |\like |\Grb-2. |(activation |\of |\Grb-2 |\leads |\to |
recruitment |\of |\SOS |\and |\activation |\of |\Ras) What |\is |\Ras? |- |\CORRECT |\ANSWERS |\✔✔A |\small |\monomeric |\G- protein |\anchored |\to |\the |\inner |\PM |\involved |\in |\many |\signalling |
responses |\when |\activated |\to |\trimeric |\G-protein. What |\is |\Ras |\regulate |\by? |- |\CORRECT |\ANSWERS |\✔✔Ras |\is |
regulated |\by |\guanine |\nucleotide |\exchange |\factor |(GEF) |\and |
GTPase |\activating |\proteins |(GAPs). |\Ras |\switches |\between |\active |
and |\inactive |\states. |
Ras |\G |\protein |\inactive |\bound |\to |\GDP. |\
GDP |\is |\exchanged |\for |\GTP |\by |\GEFs |\and |\Ras |\is |\activated. |
GAPs |\accelerate |\OFF |\by |\enhancing |\the |\hydrolysis |\of |\GTP |\to |\GDP. What |\happens |\when |\Ras |\proteins |\are |\mutated? |- |\CORRECT |
ANSWERS |\✔✔Mutated |\Ras |\proteins |\are |\unable |\to |\dissociate |\GTP, |
so |\they |\are |\stuck |\in |\the |\ON |\or |\proliferative |\state. |\Can |\lead |\to |
cancer. What |\happens |\when |\Ras-GAPs |\when |\they |\are |\mutated? |- |
CORRECT |\ANSWERS |\✔✔Mutations |\lead |\to |\disease |\because |\the |
Ras-GAPs |\proteins |\can't |\hydrolyze |\GTP |\back |\to |\GDP |\efficiently |\so |
Ras |\stays |\activated |\longer |\than |\it |\should. What |\is |\SOS? |- |\CORRECT |\ANSWERS |\✔✔Is |\a |\guanine |\nucleotide |
exchange |\factor. How |\is |\Ras |\linked |\RTKs? |- |\CORRECT |\ANSWERS |\✔✔An |\adaptor |
protein |(Grb-2) |\and |\a |\GEF |(SOS) |\link |\activated |\RTKs |\to |\Ras |
(downstrea |\signalling |\proteins). What |\is |\Grb-2? |- |\CORRECT |\ANSWERS |\✔✔Grb-2 |\is |\a |\adaptor |
(linker) |\protein |\that |\couples |\activated |\RTKs |\to |\downstream |
signalling |\proteins |\like |\Ras. What |\is |\Grb-2 |\composed |\of |? |- |\CORRECT |\ANSWERS |\✔✔Composed |\of |\SH2 |\and |\SH3 |\domains.
What |\is |\Raf? |- |\CORRECT |\ANSWERS |\✔✔Is |\a |\MAPKKK. |\Ras- Associating |\Factor. |\Serine/threonine |\kinase What |\is |\the |\activation |\of |\Raf |\associated |\with? |- |\CORRECT |
ANSWERS |\✔✔Activation |\is |\associated |\with |\several |\proteins:
- |\serine/threonine |\phosphatase |\P2A
- |\Hsp90 |\chaperone |\heat |\shock |\protein
- |\Scaffold |\protein |\14-3- What |\is |\the |\Hsp90 |\function |\in |\activation |\of |\Raf? |- |\CORRECT |
ANSWERS |\✔✔Is |\a |\chaperone |\heat |\shock |\protein. |\It |\helps |\to |
stabilize |\Raf |\and |\is |\involved |\in |\proper |\cell |\localization. What |\is |\the |\scaffold |\protein |\14-3-3 |\function |\in |\Raf activation? |- |\CORRECT |\ANSWERS |\✔✔Is |\a |\phosphoserine |\adaptor/chaperone |\protein. |\It |\locks |\Raf |\in |\its |\inactive |\formation. |
It |\interacts |\with |\the |\RBD |\N-terminal |\region |\bound |\at |\two |
phosphoserine |\residues |\on |\Raf |\to |\inhibit |\Raf |\activation. 14-3-3 |\is |\autoinhibitory. What |\is |\an |\essential |\feature |\of |\Raf? |- |\CORRECT |\ANSWERS |\✔✔The |\N-terminal |\region |\hinders |\the |\activity |\of |\the |\catalytic |\domain |\of |
Raf. |\There |\are |\a |\number |\of |\modifications |\that |\need |\to |\occur |\in |
order |\to |\remove |\the |\restraint |\on |\Raf |\to |\enable |\its |\activation. |
Scaffold |\protein |\14-3-3 |\interacts |\with |\the |\N-terminal |\region |\to |
lock |\Raf |\in |\the |\inactive |\form.
What |\is |\the |\importance |\of |\RBD |\in |\Raf |\activation? |- |\CORRECT |
ANSWERS |\✔✔It |\is |\the |\N-terminal |\regulatory |\domain |\of |\the |\Raf |
protein. |\The |\RBD |\needs |\to |\interact |\with |\RasGTP |\to |\enable |
activaiton |\of |\Raf. |\Interaction |\of |\RBD |\with |\RasGTP |\at |\the |
membrane |\destabilizes |\Raf |\interaction |\with |\14-3-3. |\This |\allows |
for |\PP2A |\to |\dephosphorylate |\Raf |\phosphoserines |(the |\locks |\on |
the |\inactive |\state). What |\is |\RBD? |- |\CORRECT |\ANSWERS |\✔✔Ras |\Binding |\Domain. |\It |\is |
the |\Raf |\N-terminal |\domain |\of |\the |\Raf |\protein. How |\is |\Raf |\maintained |\in |\an |\inactivate |\state? |- |\CORRECT |
ANSWERS |\✔✔Scaffold |\protein |\14-3-3 |\is |\bound |\to |\two |
phosphoserine |\in |\the |\N |\terminus |\on |\the |\Raf |\protein |\and |\locks |\it |
in |\the |\inactive |\form. What |\is |\the |\function |\of |\serine/threonine |\phosphatase |\PP2A |\in |\the |
activation |\of |\Raf? |- |\CORRECT |\ANSWERS |\✔✔Once |\RBD |\has |\bound |
RasGTP |\the |\interaction |\between |\Ras |\and |\14-3-3 |\destabilizes. |
PP2A |\comes |\and |\dephosphorylates |\the |\phosphoserines |\on |\the |
Ras. |\Allowing |\for |\other |\phosphorylations |\on |\Raf |\activating |\it |\and |
causing |\dimerization. How |\does |\Raf |\associate |\with |\RasGTP |\to |\become |\activated? |- |
CORRECT |\ANSWERS |\✔✔RBD |\binds |\to |\the |\activated |\Ras |(RasGTP) |
and |\causes |\the |\destabilization |\of |\the |\inhibitory |\protein |\14-3-3 |
which |\allows |\the |\PP2A |\to |\dephosphorylate |\Raf |\and |\allow |\for |\other |\phosphorylations |\on |\Raf |\that |\result |\in |\activation |\and |
dimerization.
What |\is |\MAPKK? |- |\CORRECT |\ANSWERS |\✔✔Is |\a |\dual |\specificity |
kinase: |\Has |\both |\ser/thr |\and |\tyrosine |\kinase |\catalytic |\domains. What |\is |\the |\substrate |\of |\MAPKK? |- |\CORRECT |\ANSWERS |\✔✔MAPK |
is |\the |\only |\substrate |\of |\MAPKK. |\It |\is |\a |\tightly |\regulated |\response. What |\is |\the |\function |\of |\MAPKK? |- |\CORRECT |\ANSWERS |
✔✔MAPKK/MEK |\catalyzes |\a |\phosphorylation |\event |\on |\threonine |
and |\one |\on |\tyrosine |\to |\make |\MAP-kinase |(MAPK) |\fully |\active. How |\is |\MAPK |\activated? |- |\CORRECT |\ANSWERS |\✔✔Only |\when |\both |\threonine |\and |\tyrosine |\are |\phosphorylated |\by |\MEK/MAPKK. |\It |
dimerizes. What |\is |\the |\pathway |\of |\Ras |\activation |\to |\activated |\MAPK? |- |
CORRECT |\ANSWERS |
✔✔RTK-(SH2-SH3)-SOS-Ras-(RBD-Raf/MAPKKK)-MAPKK/MEK-MAPK What |\are |\the |\six |\steps |\of |\Ras |\activation |\to |\activated |\MAPK? |- |
CORRECT |\ANSWERS |\✔✔1. |\Ras |\activated |\by |\exchange |\of |\GDP |\for |
GTP
- |\Active |\Ras |\recruits, |\binds, |\and |\activates |\Raf
- |\GTP |\hydrolysis |\leads |\to |\dissociation |\of |\Ras |\from |\Raf
- |\Raf |\activates |\MEK
- |\MEK |\activates |\MAPK
- |\Dimeric |\form |\of |\active |\MAPK |\translocates |\to |\nucleus; |\activates |\many |\transcription |\factors.
What |\is |\the |\function |\of |\MAPK? |- |\CORRECT |\ANSWERS |\✔✔Activates |\many |\transcription |\factors. |\It |\induces |\transcription |\of |\c-fos |\by |
modifying |\two |\transcription |\factors |(TCF |\and |\SRF). What |\is |\TCF? |- |\CORRECT |\ANSWERS |\✔✔A |\transcription |\factor. |
Ternary |\Complex |\factor. It |\resides |\in |\the |\nucleus. What |\is |\the |\function |\of |\TCF? |- |\CORRECT |\ANSWERS |\✔✔TCF |\is |\a |
transcription |\factor |\activated |\by |\phosphorylation |\by |\MAPK. |\It |
binds |\enhancer |\element |\SRE |\regulating |\c-fos |\and |\other |
transcriptional |\events What |\is |\SRF? |- |\CORRECT |\ANSWERS |\✔✔Serum |\response |\element. |
SRF |\is |\a |\transcription |\factor. What |\is |\the |\function |\of |\SRF? |- |\CORRECT |\ANSWERS |\✔✔MAPK |
phosphorylates |\and |\activates |\the |\kinase |\p90Rsk |(in |\cytosol) |
which |\translocates |\to |\the |\nucleus |\and |\phosphorylates |\nuclear |
SRF |(transcription |\factor). |\This |\increases |\the |\binding |\rate |\and |
affinity |\of |\SRF |\binding |\to |\SRE |= |\increased |\transcriptional |
frequency. What |\is |\the |\pathway |\of |\regulation |\of |\transcription |\activated |\by |
MAPK? |- |\CORRECT |\ANSWERS |\✔✔MAPK |\phosphorylates |\p90Rsk |
which |\phosphorylates |\SRF |\and |\MAPK |\also |\phosphorylates |\TCF |
which |\both |\are |\trasncription |\factors |\that |\bind |\to |\the |\SRE |\
What |\is |\Her2/neu/ErbB-2? |- |\CORRECT |\ANSWERS |\✔✔RTK |\of |\EGF |
class. What |\is |\EGF? |- |\CORRECT |\ANSWERS |\✔✔Epidermal |\growth |\factor. |\It |\stimulates |\proliferation |\of |\many |\cell |\types. Is |\Her-2/neu/ErbB-2 |\an |\oncogene? |- |\CORRECT |\ANSWERS |\✔✔Yes. |
It |\has |\the |\potential |\to |\mutate |\and |\contribute |\to |\uninhibited |
proliferation |\and |\can |\induce |\cell |\transformation. |
It |\is |\frequently |\amplified/over-expressed |\in |\human |\tumours |\of |
epithelial |\origin. What |\happens |\when |\Her2/neu/ErbB-2(GF) |\is |\mutated? |- |\CORRECT |\ANSWERS |\✔✔Mutations |\within |\the |\TM |\region |\can |\cause |
constitutive |\dimerization |\in |\an |\activated |\state |\and |\this, |\in |\the |
case |\of |\the |\ErbB2 |\receptor |\can |\induce |\cell |\transformation. |\It |\is |\an |\oncogene. |
Frequently |\amplified/over-expressed |\in |\human |\tumours |\of |
epithelial |\origin. What |\is |\the |\amplification |\or |\overexpression |\of |\Her-2 |\recognized |
as? |- |\CORRECT |\ANSWERS |\✔✔Amplification |\of |\Her-2 |\is |\a |
recognized |\prognostic |\marker |\that |\is |\associated |\with |\poor |
survival |\for |\patients |\with |\node-positive |\breast |\cancer. Why |\is |\mutation |\not |\necessary, |\but |\overexpression |\of |\Her-2 |
sufficient |\to |\become |\tumourigenic? |- |\CORRECT |\ANSWERS |\✔✔If |\
there |\is |\overexpression |\than |\it |\leads |\to |\ligand |\independent |
activation What |\is |\Herceptin? |- |\CORRECT |\ANSWERS |\✔✔Designer |\Cancer |
therapy. |
Humanized |\monoclonal |\antibody. What |\is |\another |\name |\for |\Herceptin? |- |\CORRECT |\ANSWERS |
✔✔Trastuzumab. |
mab |\because |\it |\is |\a |\humanized |\monoclonal |\antibody. How |\is |\Herceptin |\administered? |- |\CORRECT |\ANSWERS |
✔✔Herceptin |\is |\given |\IV. Is |\Herceptin |\only |\used |\for |\breast |\cancer? |- |\CORRECT |\ANSWERS |
✔✔No. |\It |\is |\also |\in |\trial |\for |\late |\stage |\pancreatic |\cancers |\that |
over-express |\Her2/neu/ErbB. |
It |\is |\given |\in |\combination |\with |\the |\chemotherapeutic |\drug |
Gemzar. How |\does |\Herceptin |\function? |- |\CORRECT |\ANSWERS |\✔✔It |\binds |
to |\Her-2 |\and |\blocks |\its |\activation. How |\can |\mutated |\Ras |\result |\in |\cancer? |- |\CORRECT |\ANSWERS |
✔✔Mutated |\Ras |\can |\make |\Ras |\insentitive |\to |\GAP |\binding, |\so |\GTP |
can't |\be |\hydrolyzed |\to |\GDP. |\This |\results |\in |\permanent |\activation. |
Resulting |\in |\unihibited |\cellular |\proliferation.
membrane |\then |\this |\will |\block |\signalling |\associated |\with |
abnormal |\cell |\division. What |\is |\another |\target |\therapy, |\other |\than |\Her2 |\inhibition? |- |
CORRECT |\ANSWERS |\✔✔FTase |\inhibitors. |\It |\also |\blocks |\cellular |
proliferation. What |\is |\Lonafarnib |\and |\Tipifarnib? |- |\CORRECT |\ANSWERS |\✔✔They |
are |\farnesyl |\transferase |\inhibitors. What |\is |\Rigosertib? |- |\CORRECT |\ANSWERS |\✔✔It |\is |\a |\drug |\that |
prevents |\Raf/Ras |\interactions |\to |\block |\the |\MARK |\signalling |
pathway |\to |\inhibit |\tumourigenic |\proliferation. What |\is |\the |\function |\of |\Rigosertib? |- |\CORRECT |\ANSWERS |\✔✔It |\is |
a |\small |\molecule |\that |\binds |\to |\the |\RBD |\N |\terminal |\of |\Raf |\and |
prevents |\its |\association |\with |\Ras. What |\are |\three |\therapeutic |\targets |\in |\the |\RTK/MAPK |\pathway? |- |
CORRECT |\ANSWERS |\✔✔HER2 |- |\Herceptin |\binds |\to |\the |\RTK |\and |
prevents |\cellular |\proliferation FTase |\Inhibitors |- |\Lonafarnib/Tipifarnib |\inhibits |\Ras |\from |\binding |
to |\the |\inner |\membrane |\and |\prevents |\proliferation RBD |\of |\Raf |- |\Rigosertib |\is |\a |\molecule |\that |\binds |\the |\N |\terminal |
and |\prevents |\RAS |\from |\binding |\to |\the |\RBD |\of |\Raf.
How |\is |\PI3-K |\activated? |- |\CORRECT |\ANSWERS |\✔✔They |\are |
activated |\by |\binding |\to |\specific |\phospho-tyrosines |\on |\activated |
RTKs. What |\is |\the |\ultimate |\goal |\of |\PI3-K? |- |\CORRECT |\ANSWERS |\✔✔It |
initiates |\the |\activation |\of |\a |\major |\intracellular |\signalling |\pathway |
that |\promotes |\cell |\survival. |
PI3-K |\is |\responsible |\for |\the |\activation |\of |\Akt. What |\does |\PI |\stand |\for? |- |\CORRECT |\ANSWERS |
✔✔Phosphatidylinositol What |\is |\Atk |\also |\known |\as? |- |\CORRECT |\ANSWERS |\✔✔Protein |
Kinase |\B. |\PKB What |\are |\the |\components |\of |\PI3-K? |- |\CORRECT |\ANSWERS |
✔✔There |\are |\ 2 |\subunits; |\a |\regulatory |\subunit |(p85, |\with |\SH2 |
domain) |\and |\a |\catalytic |\subunit |(p110). What |\is |\the |\characteristics |\of |\p85 |\subunit |\of |\PI3-K? |- |\CORRECT |
ANSWERS |\✔✔There |\are |\two |\SH2 |\domains, |\an |\N-terminal |\and |\a |\C- terminal |\domain |\that |\recognize |\phosphorylated |\tyrosine |\motifs. |
There |\is |\consesnus. What |\is |\Akt? |- |\CORRECT |\ANSWERS |\✔✔It |\is |\a |\serine/threonine |
kinase.
