lec 14-15. vesicular trafficking Flashcards

1
Q

orientation in biological membranes

A
  • membranes stay the same

- lipids flip

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2
Q

SNAREs

A

provide specificity in vesicle targeting

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3
Q

ER translocation

A

moving proteins from cytosol into ER

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4
Q

RER vs SER

A

RER - has ribosomes which synthesize proteins

SER - makes lipids and trigylceries, stores Ca+

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5
Q

co-translational translocation

A

protein is being put into the ER while being translated

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6
Q

post-translational translocation

A

protein is made by ribosomes, folded by chaperones, then moved into an organelle
(sometimes ER, but more common mitochondria, peroxisomes, chloroplast)

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7
Q

signal hypothesis

A

ER translocated requires a signal, so if a protein has an amino acid sequence encoding a signal sequence, then it can be translated + cotranslated

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8
Q

how a protein is translocated

A

the signal sequence on the n-terminus anchors it into the membrane, while the rest of the protein goes into the lumen through the translocator (Sec61). Then signal sequence is cut off with signal peptidase and translocator shuts

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9
Q

how a membrane protein is translocated

A

they have an additional stop-transfer sequence in the middle (TMD) which tells the translocator to close

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10
Q

types of membrane protein

A

type 1 - N-terminus in lumen

type 2 - C-terminus in lumen

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11
Q

BIP

A

an ER chaperone that associates with new antibodies and makes sure they stay in lumen until correctly assembled

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12
Q

diseases associated with misfolded proteins

A
cystic fibrosis
gauchers
emphysema
liver damage
hypothroidism
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13
Q

essential components of COPII for vesicle formation

A

1) GTPase (Sar1)
2) adaptor proteins (sec23/24)
3) coat (13/31)
4) ATP and GTP

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14
Q

GTPases in vesicle formation

A

inactive GDP (Sar1-GDP) is converted into active GTP (Sar2-GTP) by GEF. The active GTP and interact with other proteins - it recruits adaptors and identifies the ER exit site

GTPase with the help of GAPs can then convert GTP back into GDP

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15
Q

adaptors

A

recognise and select cargo + link the transmembrane cargo to the outer coat.
they work by recognising the messages in cytoplasmic domains of membrane proteins

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16
Q

coats

A

provide structural scaffold and enable pinching

17
Q

cranio-lenticulo dysplasia

A

caused by Sec23A (adaptor) mutation which affects ER-> Golgi trafficking
have problems with secreting large cargo like collagen
only some tissues are affected because Sec23B acts redundantly to compensate