Endomembrane system Flashcards

1
Q

components of the endomembrane system (6)

A

RER
SER
Golgi
lysosomes
transport and secretory vesicles
nuclear envelope

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2
Q

How can ER fragments be isolated and obtained?

A

-centrifugation of sample at high speed
-collection of the tissue homogenate
-different homogenate samples are harvested at diff speeds and henc include different components of the cell
- MICROSOMAL FRACTION obtained: fragments (microvesicles) of the ER called microsomes
-staining and microscopy for visualisation (RER microsomes have dark ribosomes in the sample that are absent in SER)

!! usually SER microsomes have a lower density (and hence are found abive) RER microsomes

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3
Q

morphology of SER

A

-no ribosomes on membrane (hence no involvement in protein synthesis)
-tubular arrangement
-membrane bound

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4
Q

General functions of the SER (5)

A
  1. lipid/steroid synthesis and metabolism
  2. compound detoxification
  3. glycogen metabolism
  4. Ca2_ storage
  5. biogenesis of cell membranes
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5
Q

process by which SER detoxifies compounds

A

usually by the addition of OH groups to toxic compounds, favouring their elimination

!!! very frequent in liver cells

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6
Q

process of plasma membrane biogenesis occuring in SER

A

-lipids (that form part of phospholipids) are synthesised by enzymes in SER
-phospholipids inserted into the cytosolic leaflet of membrane bilayer
- composition of bilayer odified by 2 ENZYMES:

  1. scramblase: restores the same number of PLs in layers
  2. flipase/flopase: flips phospholipids to have specific PL composition on each layer as needed

!! both these enzymes are transmembrane

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7
Q

purpose of Ca2+ storage achieved by SER

A

-monitors the ratio of calcium accummulation and release from/into cytoplasm

!! VITAL IN SKELETAL MUSCLE CELLS:
-SER is called sarcoplasmic reticulum
-Ca2+ ions allow muscle contraction
-SR releases Ca2+ upon depolarisation to contract muscle
-SR uptakes Ca2+ when the signal is done to stop contractions

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8
Q

process by which SER synthesises steroids and lipids

A

!!occurs in gonads and adrenal gland
-cooperation with mitochondria

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8
Q

process by which SER metabolises glycogen

A

OCCURS IN LIVER CELLS:
-SER used in a step of the process which degrades glycogen into glucose
-Glycogen turns into glucose-6-phosphate which cannot be transported in the bloodstream due to its connection to a phosphate group
-SER membrane contains permeases (enzymes) that remove the Pi group
-hence the compound is changed into glucose and is able to be transported in the bloodstream

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9
Q

Morphology of RER

A

-cisternae (flattened tubes)
-connected with nuclear envelope
-ribosomes on surface
-membrane bound

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9
Q

general functions of RER (5)

A

-protein synthesis
-folding of proteins into secondary and tertiary structure
-Nglucosylation modifications
-holds integrity of cell due to being connected with nuclear components
-addition of OH groups (hydroxylation) to lysine residues of tropocollagen molecules

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10
Q

RER in neurones name

A

NISSL BODIES: clumps of RER and free ribosomes in neurons
-taken as markers for these cells
-not present in axon or dendrites (only on the body where protein synthesis occurs)

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11
Q
A
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12
Q

2 areas where proteins can be synthesised and the differences between the proteins made

A
  1. synthesis on cytosolic polysomes (activated aggregates of free ribosomes):
    -nuclear proteins (TFs/histones)
    -soluble proteins (final destination being the cytoplasm)
    -mitochondrial proteins
  2. synthesis on RER bound ribosomes:
    -secreted proteins (antibodies)
    -integral membrane proteins (ion channel subunits)
    -ER, Golgi and lysosome lumen resident proteins
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13
Q

how are proteins imported into the RER

A

SRPS: signal recognising particles

-proteins incoming to RER contain signal sequence
-SRPs on membrane of RER recognises this signal sequence
-after recognition, protein moves through translocation channel and is inserted into RER lumen

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14
Q

Structure of ribosomes

A

-major and minor subunit that are assembled to form a fully active ribosome
-can either be associated with RER or be free in cytosol

Prokaryotes: 70S ribosomes, 50S major and 30S minor

Eukaryotes: 80S ribosomes, 60S major and 40S minor

15
Q

Morphology of golgi apparatus

A

-several membrane bound sacs called cisternae
-slightly curves, convex or concave depending on the region
-surrounded by vesicles (cis = transport, trans = secretory)

3 REGIONS:
1. CIS face: convex cisternae and faces the nucleus/RER.
2. TRANS face: concave cisternae and faces the plasma membrane
3. Medial golgi (central portion)

16
Q

2 complexes formed in the cis and trans face of the golgi apparatus

A

CIS FACE: ERGIC (endoplasmic reticulum-golgi apparatus intermediate compartment)

TRANS FACE: TGN (trans golgi network)

!! in these complexes, transport vesicles in CIS face or secretory vesicles in TRANS face fuse/bud off

17
Q

distribution of golgi in cell cycle

A

-duplication occurs
-fragmentation
-distribution of components to the daughter cell
-fusion in telophase to form new and rearranged cisternae

18
Q

2 types of vesicular movement

A
  1. ANTEROGRADE: vesicles fuse wih cis region, undergo modification, fuse with trans region for exocytosis
  2. RETROGRADE: ability of some vesicles to move back towards RER after reaching the trans face
19
Q

what are some possible fates of vesicles undergoing retrograde motion?

A

-they return and remain in lumen of RER or Golgi
-blended with lysosomes to be degraded
-some vesicles are empty are incorporated into plasma membrane to build it up

20
Q

general functions of golgi apparatus (6)

A

-modification via glycosylation
-activation of peptides by phosphorylation
-vesicle production
-synthesis of GAGs
-incorporation of empty vesicles to membrane
-selection of proteins that need to undergo lysosomal degredation

21
Q

ERAD trigger and detailed sequence

A

TRIGGER: removal of mannose residues from misfolded proteins

PROCESS:
1. misfolded protein is sent to retrotranslocation complex which causes retrotranslocation of the proteins from the ER lumen to cytoplasm

  1. proteins are polyubiquitinated during the retrotranslocation and end up in cytoplasm to be degraded by the proteasome system