Module 7: V1-V3 Flashcards

1
Q

Why do cells communicate?

A

survive
grow + divide
differentiate
die

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2
Q

What is signal transduction?

A

movement of signal from the outside of a cell to the inside of a cell

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3
Q

What are the different ways in which a signal is transmitted?

A

contact-dependent
paracrine
synaptic
endocrine

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4
Q

What is specificity?

A

signal molecule fits binding site on its complementary receptor; other signals do not fit

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5
Q

What is amplification?

A

when enzymes activate enzymes, the number of affected molecules increases geometrically in an enzyme cascade

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6
Q

What is modularity?

A

proteins with multivalent affinities form diverse signaling complexes from interchangeable parts
phosphorylation provides reversible points of interaction

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7
Q

Signalling molecules are usually expressed and degraded __________. (very fast / very slow)

A

very fast

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8
Q

How are molecular switches turned on / off?

A

either signaling by phosphorylation or GTP-binding

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9
Q

What are GPCRs associated with?

A

a guanine nucleotide-binding protein (G protein)

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10
Q

What type of activity does the ɑ subunit of a G protein have?

A

GTPase activity as the ɑ subunit has a GDP-binding site

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11
Q

What do the ɑ and ɣ subunits of a G protein have?

A

lipid molecules that insert into the membrane

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12
Q

What does the activation of an enzyme by a G protein result in?

A

results in increased enzymatic activity and therefore an increased signal output

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13
Q

How is a β-adrenergic receptor activated by adrenaline?

A

adrenaline binds -> G protein GDP is replaced by GTP = activation -> G protein activates adenylyl cyclase (AC) -> AC catalyses formation of cAMP -> cAMP activates PKA -> PKA phosphorylates cellular proteins = cellular response (>100,000 molecules liberated)

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14
Q

What are receptor tyrosine kinases stimulated by?

A

growth factor

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15
Q

What is the structure of a receptor tyrosine kinase?

A

a receptor coupled to an enzyme

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16
Q

What does downstream signalling of receptor tyrosine kinase stimulate?

A

survival, growth and proliferation

issues with these receptors are linked to cancer

17
Q

What is cross-phosphorylation by activated kinase domains?

A

when one receptor by itself cannot become activated but once it is paired up with a partner it can

18
Q

What is dominant-negative inhibition by receptor tyrosine kinase?

A

if one receptor is mutated and has no activity then downstream signalling is not able to occur because it cannot pair up with a partner

19
Q

How to RTK signalling pathways progress?

A

activated receptor -> phosphorylates downstream target (e.g. transcription factor) which becomes a docking site for other signalling molecules -> amplification through multiple rounds of enzyme activation

20
Q

Cell signalling is often described like electric circuitry. What key features do you think they share that make this analogy a good one?

A

both allow for the movement of a signal from one place to another
as well as this circuits and cell signalling can both be switched on or off

21
Q

Does protein phosphorylation always activate a protein. Why, why not?

A

no, because sometimes phosphorylation results in inactivation of a protein

22
Q

Does ligand binding always need to cause receptor tyrosine kinases to dimerise? What does it need to cause?

A

no, the ligand must bind to the extracellular domain