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44 Cards in this Set

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In protein-protein interaction what is bound on cell surface?
receptor bonded hormone (like adreniline for fight or flight response)
In what interaction is PKA? What does PKA stand for?
Protein-Protein, protein kinase A
1. Receptor binds hormone which 2. activates GTP binding protein 3.which activates adenyl cyclase 4.which mediates the reaction is the process of what?
Protein-protein interactions.
What is C?
What is R?
Where are these processes relevant?
C is the catalytic subunit of protein kinase A
R is the regulatory subunit that releases C when bound to cAMP
These processes happen in protein-protein interactions.
Glycogen phosphorase can be activated in minutes to make what for what?
ATP for muscles
C does what to many different proteins such as transcription factors, metabolic enzymes, etc.?
phosphorylate
cAMP-->AMP by what?
enzyme phosphodiesterase (inhibited by caffiene-like compounds)
What happens when there is a decrease in [cAMP]?
C re-associates with R and becomes inactive
Protein phosphates dephosphorylate what?
PKA substrates of another area of regulation
CREB is a transcription factor that does what?
when phospholated by PKA it binds to specific sequences in promoters of responsive genes to regulate transcription.
PKA phosphorylates Phosphorylase kinase and glycogen synthase to do what?
PKA makes Phosphorylase kinase active an glycogen synthase inactive
PKA phosphorylates Phosphorylase kinase and glycogen synthase to do what?
PKA makes Phosphorylase kinase active an glycogen synthase inactive
What activates glycogen phosphorylase ?
phosphoroylase kinase
Glycogen phosphorylase mediates the first step in glycolysis and ATP production which is
glycogen to glucose-1-phosphate
The activation of PKA promotes what? and inhibits what?
promotes glycolysis and inhibits glycogen synthesis
G proteins are slang for what?
GTP-binding proteins.
Guanine nucleotide binding are consider what?
binary switches for GTP-bound ON and GDP-bound OFF.
stimulation of exchange of GDP for GTP (from off to on) is activated by which protein?
GNRPs protein

Guanine Nucleotide Release Proteins(lacking guanine nucleotide next)
What protein is turned on to bind guanine nucleotide sites to turn the G-site on?
effector protein
GAPs stands for what? GAPs do what?
GTPase Activating Proteins, they convert bound GTP to GDP and PI and turn themselves off after interacting with the effector.
What are the three subunit classes in trimetric G-proteins?
alpha, beta, gamma
Which of the three membrane anchors do most of the work?
Alpha anchors
A common example of loe molecular weight GTP binding proteins associated with tumors is
ras is found in 30-50% of tumors in humans, other family members are rho, rab, ran
Why do proteins degrade? Which protein does not turn over?
Proteins degrade because they are starved for amino acids, histones don't turn over
How long do histones last? How about regulatory proteins? Which proteins are most targeted or destruction?
Histones (certain lens proteins) can last for years, regulatory proteins last for minutes to hours, damaged/misfolded/aged proteins are the most targeted for destruction
What are three ways proteins are recognized to be destroyed?
1. exposed hydrophobic domains
2. N-termini correlate with degregation
3. destruct box aa concentration
Destruct box PEST hypothesis is what?
sequence rich in Pro, Glu, Ser, Thr
Pro, Glu, Ser, Thr maybe the site of phosphorylation involved in what?
Degregation, clone and mutate,
or mutate and delete to find rate
ubiquitin does what?
conjugates enzymes in the protein destruction process
What does ubiquitin ligase do?
Adds more ubiquitin and makes a polyubiquitin chain and convalently attaches a side chain of lymine to make a branch chain polypeptide
What continues to be polynuclated on a polynucleated substate
ubiquitin
What is the destruction machinery what takes place there?
the Proteosome is where proteolous takes place
What are five basics of the Proteosome?
1. large (26S) complex in cyto,
2. recognizes polyubiquitin- conjugated proteins,
3. feeds proteins through with ATP-dependant unfoldase (sent to core of proteosome)
4. ubiquitin is released to be reused (cleaved off )
5. protein degregation down to aa and small pepties
Immunity regulation includes what two things
degradation and protein-protein interaction
In B-lymphocytes NF-kB is what?
an inactive transcription factor that binds IkB in the cytoplasm
Activation of a protein kinase that phosphorylates IkB happens in what kind of cell?
B-cells (antigen-presenting cells)
Phosphorylated IkB is targeted by what?
ubiquitin-conjugating enzymes
What produces signaling proteins which are released into the blood to activate T-cells?
NF-kB translocates to the nucleous to activate these genes to produce the proteins.
What produces signaling proteins which are released into the blood to activate T-cells?
NF-kB translocates to the nucleous to activate these genes to produce the proteins.
What produces signaling proteins which are released into the blood to activate T-cells?
NF-kB translocates to the nucleous to activate these genes to produce the proteins.
By binding a calcium-binding protein called calmodulin a phosphatase is activated when what happens?
T-cells become activated
By binding a calcium-binding protein called calmodulin a phosphatase is activated when what happens?
T-cells become activated
By binding a calcium-binding protein called calmodulin a phosphatase is activated when what happens?
T-cells become activated
What produces signaling proteins which are released into the blood to activate T-cells?
NF-kB translocates to the nucleous to activate these genes to produce the proteins.