Golgi Flashcards

1
Q

Golgi do to glycoprotein and membrane lipid

A

Process and sort them
Glycosylation and processing of carbohydrates side chain occurs, then distributed to other locations

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2
Q

What happens to proteins released into ER lumen

A

Golgi apparatus
Secretory vesicles
Lysosome
Back to ER

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3
Q

CGN

A

Sorting of proteins to be sent back to ER or on the golgi

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4
Q

TGN

A

Segregating proteins into vesicles headed to plasma membrane

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5
Q

Terminal glycosylation

A

Occur in golgi
Modification of glycoproteins through removal/addition of sugar side chain on the core oligosaccharide (added in ER)
Happen on luminal side

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6
Q

Great diversity of type of glycosylation because ———

A

Enzyme being very specific for certain carbohydrates

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7
Q

Each step of glycosylation depends on

A

Presence of previous carbohydrates
That why it is critical

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8
Q

Glycosylation is a ——— process

A

Linear

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9
Q

Glycosylation function

A

-proteins/lipid sorting
-makes glycoproteins more resistant to digestion by proteases
-recognition molecule in cell-cell interaction
-regulatory roles

GOVE CELL ABILITY TO GENERATE MANY CHEMICALLY DIFFERENT MOLECULES

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10
Q

Movement through golgi

A

1- stationary cisternae model
2- cisternal maturation model

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11
Q

Stationary cisternae vs cisternal maturation

A

Stationary:
Cisternae and resident s enzymes stay in place while cargi move forward
cargo would be found in vesicles
#there would be little change in golgi structure
++ealry and late golgi proteins would never co localize
Cisternal:
Cargo remain in cisternae while cisternae move forward
resident enzyme found in vesicles
#golgi would disappear
++ cisternae would express early then late resident proteins

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12
Q

Movement of material toward plasma membrane

A

Anterograde transport

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13
Q

Movement of material toward ER

A

Retrograde transport

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14
Q

Sorting of proteins

A

Begin in ER
Final sort in TGN

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15
Q

Protein Targeting

A

—Protein synthesized on RER must be directed to variety location
—Each protein has specifc tag targeting it to transport vesicle that take ot to correct location

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16
Q

Protein residency

A

Proteins are kept by two mechanisms
Retention and Retrieval

17
Q

Retention

A

Resident molecules are excluded from transport vesicles

18
Q

Retrieval

A

Tags can be used to return escaped proteins

19
Q

Tags on proteins

A

Depends on proteins and destination
Tag can be amino acid sequence, hydrophobic domain or oligosaccharide side chain

20
Q

Protein composition of ER is maintained by

A

1- preventing proteins from escaping
2- returning others from golgi

*these proteins don’t need targeting sequence since they were synthesized in ER

21
Q

retention and retrieval is done by

A

1- soluble ER specific proteins
2- ER specific transmembrane proteins

22
Q

Soluble ER specific proteins

A

Most common ER retention tag is KDEL retrieval signal that mediate the return of soluble proteins to ER

23
Q

KDEL retrieval signal

A

C-terminal amino acid sequence

24
Q

ER-specific transmembrane proteins

A

Membrane proteins have Retention signals on their cytosolic domains which binds to vesicle coat proteins, facilitate their return to ER

25
Q

ER specific transmembrane Proteins

A

KKXX

26
Q

KDEL proteins are

A

ER residents

27
Q

If KDEL proteins escape to golgi

A

1- associate with KDEL receptors (efficient binding in low ph of gogli)

2- KDEL receptor package KDEL proteins in ER-bound transport vesicle

3- KDEL receptors release proteins in the ER (binding is inefficient in high ph of ER)

28
Q

Targeting to lysosome

A

Soluble lysosomal enzymes undergo n-glycosylation followed by removal of glucose and mannose in ER and early golgi
Then phosphrylated in golgi

Forming mannose-6-phosphate tag

29
Q

Mannose-6-phosphate tag

A

Ensure delivery of lysosomal proteins to lysosome

30
Q

Mannose-6-phosphate receptor

A

Mannose-6-phosphate tag and the enzyme bind to receptor

In low ph, dissociation of enzyme and receptor

Receptor is recycled