Cellular communication and more proteins EXAM 1

Evolution Ecology And Organismal Biology 415 with Bronson at Ohio State University - All Campuses

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By: Katelyn Heath
Created: 2011-01-26
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2 Ways ER processes proteins

Glycosylation and Folding

What are oligosaccharides tags used for in the folding process of the ER?

To monitor proces

ER folding of proteins: What are partially folded glycosylated proteins bound by?

membrane or soluble proteins

What NZ monitors folding in the ER?

Glycosyl transferase

What percent of proteins gets misfolded in the ER? and then what happens?

80%, so they are taken to the cytosol destroyed and folded again

How does the ER recognize misfolded proteins?

It the tags don't match

What is ER the major source of for the cell?

all membrane phospholipids and cholesterol

Where are the NZ's for lipid synthesis found?

On the ER membrane, with active sites on cystolic side

Why are translocaters needed in the ER?

Needed because heads of the lipids have a hard time trying to flip flop to make symmetrical

2 traslocaters, where they are, and their functions

Scramblase, ER, balances density (makes more symmetrical)

Flippase, PM, sets asymmetry

What two things help Flippase do its job?

pt-ETH and pt-SER on cystolic side

How do the mechanisms of ER vesicular transport differ with direction?

THey don't

What three structures organize protein coating on bud?

Clathrin, COPI, and COPII

What does Clathrin do?

Tages buds to go from Golgi to PM

What does COPI do?

Tags buds to go from Golgi to ER

What does COPII do?

Tags buds to go from ER to Golgi

What do SNARES do?

Catches vesicles so it can go into PM, mediates fusion, and incorporates cargo proteins

What does a V snare do?

Indicates cargo and origin

What does a t SNARE do?

it matches with v SNARE at target

What feature does SNARES havefor target?

Selectivity

What are the steps of vesicles and snares for ER transport?

Incorporate cargo protein( hold cargo inside), fuse with correct target, release cargo, retrieve or recycle components

What things move into the Golgi from the ER?

ER proteins, ER lipids, and COPII which checks for folding

What things stay in the Golgi from theER?

Carb synthesis, and proteoglycans

What things leave the Golgi that were originally recieved from the ER?

Misplaced ER proteins via COPI, processed proteins going to the PM, Lysosomes or secretory vesicles

What things move from golgi to lusosomes?

NZs like hydrolase, proteases (break down proteins), and lipases (break down lipids)

How are things that are moved from golgi to lysosomes transported?

As precursors or as inactive states

What is transport from Golgi to lysosome dependent on?

M6P receptor

What happends to M6P at low pH?

It dissociates

How do things move from EC to lysosome?

Via endosomes

How does the stuff inside the endosomes going from EC to lysosomes get back to Golgi?

Endosomal proteins

Autophagy

Digestion of cellular (self-eating)

Phagocytosis

Digestion of large extracellular stuff

From Golgi apparatus to secretory pathaway what does divergence in trans golgi mean?

Don't know yet... look it up

What does constitutive secretion consist of?

Continuous, in all cells

What are the functions of constitutive secretion?

Release proteins, and replace membrane

Why does the PM need to be replaced sometimes?

Becasue exocytosis and endocytosis take soem proteins

Regulated Secretion happens in? Where are the proteins storesd? and what is the secretion based on?

Regulated secretion happens in select secretory cells, the proteins are stored in vesicels, and the secretion is based on EC signal.

4 Forms of extracellular signals

Contact dependent, paracrine, synaptic, and endocrines

Contact-dependent signals have what characteristics

They are membrane bound and not released

Paracrine signals have what characteristics?

Released but only can release to neighbors(movement based on diffusion)

Autocrine

Releases signal to itself

Synaptic signals characteristics

released, only to SPECIFIC neighbors

Endocrines signals characteristics

Relased and moves through plasma

What do Receptors do?

Bind the signal/ligand which creates an activation

Specificitiy

Can this receptor bind this particular ligand?

Affinity

Able tobind ligand but how well does it bind

Competitiors

Binding to a receptor like a ligand woud

Agonist

Acts the same as a ligand and allows the pathway to go

Antagonist

Binds to the receptor but blocks the pathway

Two types of receptors

Membrane bound receptors, intracellular receptors

Populations of receptors vary by

Cell type, stage of development, and stage of cell cycle

Signal transduction

The cells response to a signal being boudn

Why can there be 1 signal and many responses?

Different receptors and different pathways

Other signals present when another signal happens can help to

Integrate, and regulate or fine tune the response

What happens when a receptor does get signals?

There is a response, they can go kill themeselves

where are the two places intracellularly receptors can be?

in cytosol or nucleus

What are some of the problems with intracellular receptors?

Signal must get ther, so it must cross the PM

What are the best ways to get to an intracellular receptor?

Come from nearby, or with a binding protein for long distances since nonpolar doesn't like polar

What is the result of a signal getting to an intracellular receptor?

Alters DNA transcription

Why does it alter DNA transcription when an intracellular receptor binds with a signal?

Because th recptor has DNA binding region

Activation that turns into promoter

Factor

Activation that turns off promoter

Suppressor

Advantages of cell surface or membrane bound receptors

signal must only get to the receptor, it doesn't have to enter cell and can be large and polar

3 Types of receptors based on response

Ion-channel linkedrescptor

G-protein linked

Enzyme linked

What happens with an ion channel linked receptor

binding open/closes)

What happens with a G-protein linked receptor?

(binding activates G G->outer M protein (NZ or ion channel))

What happens with an enzyme linked receptor?

(binding activates receptor and enzume) or recepter go an activates a different enzyme)

How are different signals integrated to make cell signaling?

Many are needed to activate protein, each activates a different subunit

Intracellular signalin proteins are ussually activated by

Phophorylation or GTP binding

How do you turn pathways on and off for signaling?

There has to be sensitibity to signal regulated by # of receptors

What does receptor avaliability influence?

Cell activity and cell signal pathways

5 Ways to change receptor availiability

Sequester receptor (pull it in the cell)

Destroy receptor (only option for intracellular)

inactivate receptor (shape change possibly)

Inactivat intracellular signaling protiens

Activate inhibitor

About this deck

By: Katelyn Heath
Created: 2011-01-26
Size: 72 flashcards
Views: 8

About StudyBlue

“I have used this website for three exams, and I see a huge difference in my test results.”
Naj