cells and genes new content for final Flashcards
Endocrine
signaling cell and target cell are relatively distant (ex=hormones)
Paracrine
signaling cell and target cell are relatively close (ex=inflammation)
Autocrine
signal released from a cell acts on itself (ex=neurotransmitters)
Contact dependent
direct contact between membrane bound signal molecule and receptor protein on neighboring cells (developmental inhibition)
- Describe how the response of a cell is dependent of the receptors expressed
Signals bind specific receptors, most signals act on more than one type of receptor, distribution of type of receptors determine what signals a cell can respond to
- Generally describe the differences in mechanisms of how fast and slow responses occur in
Cells
Speed depends on the way a cell responds to a signal.
Fast:responses that involve secretion, cell movement, or metabolism
Slow:responses that require changes to gene expression such as increased cell growth and division
- Predict if a signaling molecule will act on extracellular or intracellular receptors based on its
Properties
1:large or hydrophillic molecules=don’t cross the membrane, extracellular signal molecule binds to cell surface receptors
2:hydrophobic molecules=can cross membrane, bind intracellular receptor
- Describe the 4 ways intracellular signals can interact in a signaling pathway
- Relay – Simple one-to-one transduction from the
receptor protein once it has bound the signal molecule. - Amplify – Each subsequent step increases in response,
making it stronger
* Few signal molecules can invoke a large response. - Integrate - Receive signals from more than one
intracellular signaling pathway and integrate them before
passing along the signal. - Distribute – one signal can activate several diverging
signaling pathways or effector proteins to create a
complex response.
- Describe what is meant by enzymes activated ‘like switches’ and the 2 ways they are
Regulated
Proteins used in intracellular signaling can be toggled between active and inactive states and remain active until turned off.
1.phosphorylation:covalent modification with addition/removal of phosphate group
2.GTP binding protein:activated with GTP bound, inactive with GDP bound
- Compare the 3 types of cell surface receptors
1.Ion channel, receptors themselves are ion channels
2.G protein coupled, membrane bound GTP binding proteins link receptor with changes inside cell (open/close ion channels, alter intracellular enzyme activity
3.enzyme coupled, binding of ligand to receptor changes enzyme activity of receptor or associated enzyme
- Describe the speed and general effect when a ligand binds an ion channel receptor
Extremely fast, changes shape, allows flow of ions across the membrane
- Describe the components and general mechanism of G protein coupled receptors
(GPCR)
Receptor bound to heterotrimeric
-ligand binding to receptor causes G protein to dissociate
-3 components can each alter distinct signaling pathways
-change enzyme signaling or can directly open an ion channel
receptors=single protein with 7 transmembrane spanning domains
-largest family of receptors
-slower than ion channels
- List the 2 ways a GPCR can alter cell function
Change enzyme signaling or can directly open an ion channel
- Define second messengers
Additional intracellular signaling molecules, they rapidly diffuse away from their source to spread signal
- Describe how cAMP can alter cell function, including how it is activated and deactivated
Inactivation of cAMP catalyzed by cyclic AMP phosphodiesterase, cyclic AMP activates cyclic AMP dependent protein kinase which catalyzes phosphorylation of proteins altering their activity
- Describe the general structure of a typical enzyme coupled receptor
Single transmembrane spanning domain
-single alpha helix
-single extracellular ligand binding domain
-cytoplasmic domain has enzyme activity or interacts with another molecule
- Describe how receptor tyrosine kinases may lead to gene transcription using (and
defining) the following terms:
Extracellular domain, intracellular domain, dimerization, phosphorylation, Ras, MAP Kinase,
transcription factors
Ligand binding causes two receptor proteins to come together (dimerization)
-contact between two activates their kinase activity
-each receptor phosphorylates each other
-newly phosphorylated tyrosine serves as binding site for intracellular signaling proteins
Protein complexes on cytosolic tails transmit signal along several routes simultaneously to many places in cell
Ras activates a phosphorylation cascade in which serine/threonine protein kinases phosphorylate and activate one another in sequence
-carries signal from PM to nucleus
-Ras activates MAP kinase kinase kinase
-MAP kinase phosphorylates various effector proteins including transcription regulators, altering gene expression
- Describe the two ways receptor tyrosine kinase activity is stopped.
1.tyrosine phosphorylation is reversed by protein tyrosine phosphatase
2.RTKs are inactivated by being endocytosed into the cell and digested by lysosomes