Lecture 17 Part 2 - Golgi Apparatus And Vescicular Transport Flashcards

1
Q

State the characteristics of Golgi complex

A

1- stack of flattened sacs (cisternae) similar in RER
2- located between the endoplasmic reticulum and the cell surface
3- divided into several compartments
4 - called the sorting post

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2
Q

Polarity of golgi complex

A

Cis face of the golgi faces the ER - receiving end of golgi

The trans face is on the opposite side of the stack- exiting side of golgi

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3
Q

Functions of golgi

A
  • sorts proteins for export to other secretory pathway organelles or outside of the cell
  • to Make Glycoproteins- add sugar to proteins
  • make complex carbohydrates to be exported from the cell ( especially in plants )
  • modifications
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4
Q

Golgi is named after

A

Camillo golgi

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5
Q

Which cell doesn’t have Golgi

A

RBC

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6
Q

Function of receiving end of golgi ( CGN )

A

Sorts proteins from the ER to the next Golgi station

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7
Q

Function of trans Golgi network ( TGN)

A

Sorts protein either TO the membrane or various other intracellular destination

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8
Q

Golgi composition

A

The composition of golgi is not uniform
And varies between cis and trans face
Different enzymes and different proteins

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9
Q

Where are most of the vescicles found

A

Exit sites of RER , they are also usually devoid of ribosomes

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10
Q

What are the 4 componenets of Golgi complex?

A

1- Cis - cisternae
2- medial - cistetnae ( bte cis and trans)
3- trans cisternae
4- trans Golgi network
The composition of these 4 compartments is very different from each other eg diff enzymes and proteins

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11
Q

Describe the movement of vescicles from ER to Golgi complex .

A

1- ER proteins are surrounded by a membrane to form the vescicles
2- transpprt vescicles fuse with one another and form the ERGIC ( endoplasmic reticulum golgi interediate compartement )
- vasicles move along the cytoskeleton ( microtubles )
- the vescicles fuse with golgi aparatus on the cis face and form the cis cisternae .
3- as proteinz move along - get modified by golgi specific enzymes
4- these modifications provide the signal for the final destination of the protein

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12
Q

Gradual movement of cisternae

A
Cis - cisternae
Goes further and fuses to form
Medial cisternae
Goes further and fuses to form
Trans cisternae
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13
Q

What are the two ways in which proteins travel through the cisternae?

A

1- vesicles that shuttle between its individual cisternae

2- maturation process- migration of Golgi cisternae through the stack

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14
Q

How proteins in vescicles move within EM

A

1-inward endocytic pathways (endocytosis)

2- outward secretory pathway (exocytosis)

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15
Q

Endocytosis ( into plasma membrane to lysosome)

A

Extracellular molecules are ingested in vescicle ( made from plasma membrane) and these molecules are then delivered to early endosomes and then to lysosome by late endosome

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16
Q

Exocytosis (from er to other organelles eg lysosomes or outside the plasma )

A

Protein molecules are transpprted from ER , through the golgi apparatus to the

  • plasma membrane through vescicles
  • to lysosome via early and late endosome - for misfolded proteins
17
Q

Cytosolic and noncytosolic sides

A

The membrane of each compartment or vesciclr maintains its orientation
Eg - the cytosolic side of membrane always faces the cytosol and non cytosolic always faces the lume

18
Q

Who is Dr randy

A

Randy schekman did a ground breaking research on cell membrane vescicle trafficking

19
Q

Vescicle budding is deriven by ————–

A

Assembly of protein coat

20
Q

What is the functions of protein coat

A
  • Causes the membrane to curve and form a vescicle

- select the components to be carried by vescicle

21
Q

What are the 3 main types of vesicles?

A

The coated Vesicles are:-

  • COP I ( coat protein)
  • COP II
  • Clatherin
22
Q

Clatherin coated - ( clatherin + adaptin 1)

A

Golgi to lysosome( via endosomes) and plant vacuoles

23
Q

Clatherin ( clatherin+ adaptin 2)

A

Plasma membrane to endosomes ( endocytosis)

24
Q

COP II

A

ER -> ERGIC -> cis Golgi -> trans Golgi

25
Q

COP I

A

TGN -> CGN -> ERGIC -> ER

26
Q

Vesicle budding and protein traffic

A

Buds
Transport
Thetering and docking
Fusion

27
Q

Describe the formation of the Clatherin coated vesicles

A
  • know that the outer membrane is made of clatherin
  • a Clatherin coated pit forms
  • self assemble into a basketlike structure on the cytosolic side
  • dynamin ( GTP binding protein- a protein to which GTP and GDP binds ) covers around the ring. Dynamin and other proteins constricts the neck
  • clatherin then pinches is off
28
Q

What is the function of adaptins ?

A

Select the cargo for transport in the vesicles

29
Q

Explain how adaptins select their cargo molecules in endocytosis

A

The cargo binds to the cargo receptor ( embedded in the membrane ) from outside the cell
Adaptin binds to the cargo receptor from inside the cell
Clatherin binds on top of the adaptin
Dynamin assembles around the forming ring , swaps GTP to GDP , and with the help of other proteins constricts the neck
Clatherin pinches the vesicles off
Once pinched off , the clatherin molecule disassemble .

30
Q

Describe the transport of vesicles to the target organelles ( eg golgi )

A

Tethering proteins, Rab proteins , and Snare proteins direct the vesicle,es to the target proteins

1- tethering protein on the target membrane binds to the Rab protein on the vesicle
2- the vesicle docks toward target
3- t snare on target binds to the v snare

31
Q

Describe the fusion of vesicle to the target .

A

Snare proteins catalyze the fusion
The binding of the snare proteins causes
- docking toward the target and draws the two lipid bilayers into close together
- the winding also forces any water out to allow a continuous fusion of lipid bilayer
- other proteins are recruited to help in fusion
- once done SNARES are pried apart for reuse

32
Q

Further modification - glycosylation in Golgi

A

2 type of glycosylation occurs in golgi

1- N- linked glycoproteins

  • removal of sugars added in RER
  • sugars added to N of asparagine

2- O- linked glycoproteins
Adding sugars to OH core of serine or threonine.

33
Q

Advantages of glycosylation

A
  • protein more hydrophilic
  • allows protein to bind to Extracellular matrix
  • reduce susceptibility to proteases
  • provide another level of structural complexity, giving it
  • new function
  • more specificity in interactions with protein.