Sorting, the RER, and the Golgi Flashcards

1
Q

Signal peptides

A

N-terminal extensions composed of 5-30 basic/hydrophobic AA

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2
Q

Signal patches

A

Distant parts of protein sequence brought together upon folding

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3
Q

Types of translocation

A

Post-translationally (C)

Co-translationally (N)

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4
Q

Post-translational translocation characteristics

A

SOluble and posses patch or signal peptide

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5
Q

Sorting into the nucleus

A
Uses NLS (short, basic squences on N-terminus of proteins)
Importin comes in with protein, uses Ran-GTP to get out
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6
Q

Sorting into mitochondria process

A

Precursors protein with MTS…binds receptor…moves to protein translocator…pulled into protein and signal sequence cleaved by peptidase

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7
Q

Sorting into mitochondrial membrane

A

Matrix targeting sequence binds TOM protein of outer…pulls through into TIM…TIM recognizes the intermembrane space-targeting sequence and diffuses over to protease…protease will cleave the matrix targeting sequence and the intermembrane space targeting seqence stays in inner membrane

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8
Q

Intermembrane space sorting

A

Intermembrane space targeting sequences pass through Tom receptor

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9
Q

Outer membrane mitochondrial proteins sorting

A

Hydrophobic transmembrane signal…recognized by TOM, passed to SAM, mim and mdm act and released into membrane

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10
Q

Peroxisomes sorting process

A

C-terminal and N-terminal ends…peroxisomal targeting sequence binds pex5 receptor…receptor binds pex14 receptor on membrane…moves through via pex 10 and 12

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11
Q

Co-translational translocation

A

Used for proteins that are secreted, membrane bound, resident in ER, golgi, or lysosomes

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12
Q

Signal for co-translational translocation

A

N-terminal signal of hydrophobic residues

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13
Q

Process of co-translational location

A

SRP binds to N terminal signal sequence…SRP binds to SRP receptor on ER membrane surface associated with translocon…GTPase activity of both SRP and SRP receptor results in opening of the translocon…signal peptidase claves the signal sequence

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14
Q

What is attached into the ER

A

N-linked glycosylation

Linked to asparagine - X - serine/threonine

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15
Q

What is in the ER membrane that holds the glycosylation chain?

A

Dolichol

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16
Q

Glucosidase

A

Chews the oligosaccharide attached to the protein

17
Q

ERAD system

A

Sends misfolded proteins for degradation

18
Q

Glycosylated proteins that pass ERAD

A

Encapsulated in transition vesicles and transported via anterograde transporrt

19
Q

Surface of vesicles from ER t oGOlgi coated with

A

COP2

20
Q

Modifications in Golgi

A

O-linked oligo added to serines and threonines

Mannose-6-P added to proteins goign to lysosomes

21
Q

Cis golgi network

A

Phosphorylation of oligosaccharides on lysosomal

22
Q

Cis cisterna

A

Removal of Man

23
Q

Medial cisterna

A

Removal of man and addition of GlcNAc

24
Q

Trans cisterna

A

Additon of Gal

25
Q

Trans GOlgi netowkr

A

Addition of NANA (common sialic acid)

And sortint

26
Q

Glycosylation purposes

A

Sorting
Stabilization of secreted proteins and transmembrane with extracellular domains
Biomolecule recognition

27
Q

Golgi to lysosomes

A

Binds to M6P receptor…travels in vesicle with clathrin coat to the early endosome…M6P dissociated…Endosome fuses to lysosome

Receptor recycled

28
Q

Secretory vs. transport vesicles

A

Secretory - regulated exocytosis

Transport - constitutive exocytosis