Intracellular Compartments And Protein Transport Flashcards

1
Q

Internal membranes

A

In eukaryotic cells, internal membranes create enclosed compartment that segregate different metabolic processes

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2
Q

Eukaryotic cells

A

Contain a basic set of membrane enclosed organelles (intestinal cell)

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3
Q

Protein following

A

Proteins in different cellular compartments and structures can be followed by green fluorescent protein tagging

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4
Q

GFP

A

Tagging a protein with GFP allows the resulting fusion to be tracked throughout the cell

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5
Q

Relative ratio of intracellular compartments

A

Varies depending on the cell type and it’s function

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6
Q

Hepatocytes

A

. Hepatocytes are the main cell types in the liver
Hepatocytes are the principle sites of production of lipoprotein particle (carry lipids via blood stream to other parts of the body)
Hepatocytes are involved in detoxification lipid soluble drugs and various harmful compounds by metabolism

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7
Q

Membrane-enclosed organelles import proteins by one of tree mechanisms

A
  1. Transport through nuclear pores (gated)
  2. Transport across membranes (membrane)
  3. Transport by vesicles (vesicular)
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8
Q

Gated

A

Cytosol-nucleus

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9
Q

Transmembrane

A

Cytosol- Mitochondria;peroxisome;plastids;ER

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10
Q

Vesicular

A

ER- golgi

Golgi-secretion vesicles; lysosome; endosome; cell exterior

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11
Q

Signal sequences

A

Direct proteins to the correct compartment

Often found at the N-terminus

Specialized signal peptidases remove the signal sequence from the finished protein once the sorting process is complete

Is the signaling finished the signal sequence get a signal patch

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12
Q

Nucleolus

A

Is a ribosome-producing factory

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13
Q

Cajal bodies

A

Are regions within the nucleus that are enriched in proteins and RNAs involved in mRNA processing
They are the main sites for the assembly of small nuclear ribonucleoproteins (snRNPs)

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14
Q

PML / promyelocytic leukaemia

A

Spherical structure in the nucleus
The principal organizing component of PML bodies is the PML protein

Vary in composition and have been implicated in cellular processes such as telomere lengthening and the DNA damage response

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15
Q

Nuclear speckles

A

Intrachromatin granule cluster
Nuclear domains enriched in pre mRNA splicing factors
Located in the interchromatin region of the nucleoplasm

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16
Q

Evolving of nuclear membrane and ER

A

May have evolved through invagination of the plasma membrane

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17
Q

Nuclear pores

A

Proteins enter the nucleus through nuclear pores

The inner and outer membran of the nucleus contain different protein compositions

The inner nuclear membran contain specific proteins that act as anchoring sites for chromatin and nuclear lamina

The outer membran is continuous with the membrane of the ER

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18
Q

Nucleoporin

A

Nuclear protein complexes are formed by about 30 different protein called, nucleoporins
and perforate the nuclear envelope

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19
Q

Nuclear lamina

A

Form of intermediate filament that gives structure, shape and strength to the nucleus

LMNA gene- code for A and C type nuclear lamina
LMNB gene- code for B type nuclear lamina

Mesh like structure

An attachment site for chromatin and chromatin binding proteins for regulating gene expression

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20
Q

Mutations in lamin proteins

A

Cause laminopathies
“Progeria” - a rare class of premature aging disorder
Hutchinson gilford progeria syndrome (HGPS)

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21
Q

Nuclear pore complexes (NPC)

A

The transport of molecules between the nucleus and the cytosol are the nucleus and the cytosol communicate with each other through NPC - gate transport

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22
Q

Gated transport

A

Bidirectional traffic at the nuclear envelope: import and export

Water soluble can diffuse passively through aqueous passages at nuclear pore complex

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23
Q

GTP hydrolysis

A

Energy supplied by GTP hydrolysis drives nuclear transport

Monomerik GTPase =RAN

NBS(nuclear export signal)

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24
Q

Peroxisomes

A

Contain oxidative enzymes (oxidase and catalase)
Involved in oxygen utilization
Name came from hydrogen peroxidase

  1. Peroxisomes in liver and kidney cells detoxify blood (Alkohol, organic contaminants)
  2. Involved in breakdown of fatty acids to acetyl CoA (Beta oxidation)
  3. Catalyze plasmalogen synthesis particularly important for myelination of neurons

A short signal sequence directs the import of proteins into peroxisomes

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25
Q

Peroxins

A

Participate in import that requires ATP hydrolysis

Reside on the peroxisome membrane and participate in ATP driven importing of peroxisome resident proteins and enzymes ATP hydrolysis

26
Q

Peroximal disorders

A

Disorders of Peroxisome biogenesis

Single peroxisomal enzyme/ protein deficiencies

27
Q

Disorders of Peroxisome biogenesis

A

Zellweger syndrome!
Neonatal adrenoleukodystrophy
Hyperpipecolic acidaemia

28
Q

Single peroxisomal enzyme/ protein deficiencies

A

X-linked adrenoleukodystrophy

Acryl-CoA oxidase deficiency

29
Q

Zellweger Syndrom

A

Is related to peroxisome biogenesis disorder PBD -leukodystrophies

Damage the white matter of the brain and also affect how the body metabolizes particular substance in the blood and organ tissue

Enlarged liver
Increased of copper and iron in the blood
Inability to move
Intellectual disability
Gastrointestinal bleeding prenatal growth failure

30
Q

Endoplasmic reticulum

A

Endo=within/plasmic=the cell/reticulum=net

rER = ribosome associated ER
sER = specialized in Lipid metabolism
- transitional ER = area of smooth ER from which transport vesicles carrying newly synthesized proteins and lipids bud off for transport to Golgi
-sarcoplasmic Reticulum specialized type of smooth ER that regulate the calcium ion concentration in the cytoplasm of striated muscle cells

31
Q

Function of ER

A
  • Central role in protein and lipid biosynthesis
  • Provides the space for Ca storage
  • All transmembrane proteins and secreted proteins pass through the ER lumen
  • Polypeptide chain are folded and assembled in the lumen of rough ER , disulfide bonds are formed, incorrectly folded proteins are recognized

sER-lipid biosynthesis of phosphogliserid,phosphatidylserin, cholesterol,seramide are carried out (!spingolipids in golgi, cardiolipin in mitochondria!)

32
Q

Function of sER

A

Function in several metabolic processes
-synthesis of lipids and steroids
-metabolism of carbohydrates
-attachment of receptors on cell membrane proteins, and steroid metabolism
!drug metabolism- some drugs are modified by microsomal enzymes -cytochrome P450
-contain the enzyme glucose6phosphatase

33
Q

Molecular function of the rER

A
Translocation
Export
ERAD
ER stress signaling
Ca homeostasis 
Disulfide isomerase
N linked glycosylation
34
Q

Protein folding

A

Protein fold into a conformation of lowest energy

Molecular chaperons often assist in protein folding

35
Q

Chaperone proteins

A

Act as isolation chambers that help a polypeptide
Other chaperon proteins act as isolation chambers that help a polypeptide fold
Prevent misfolded or partially assembled proteins from leaving the ER

36
Q

Proteosome

A

Misfolded or unwanted proteins are proteolytically cleaved by the proteasome

Like a small garbage-destruction machi

Small protein called ubiquitin form polyubiquitin chain by specifically binding lysines
Modify and mark proteins mostly for degradation by proteosome

37
Q

Disulfide bridge

A

Are formed in the rER by protein disulfide isomerase (PDI)

Disulfide bonds help to stabilize extracellular proteins

38
Q

N linked oligosaccharide

A

Most proteins synthesized in the rER are glycosylated by the addition of a common N linked oligosaccharide

39
Q

Transport from cytosol to ER

A

Through transmembrane transport

40
Q

Co translational process

A

Mammalian cells begin to import most proteins into ER before complete synthesis of the polypeptide chain

41
Q

Pool of ribosomes

A

A common pool of ribosomes is used to synthesis all the proteins encoded by the nuclear genome

42
Q

Membrane-bound polyribosomes

A

. can translate mRNAs encoding ER proteins

43
Q

Signal recognition particle

A

An ER signal sequence and an SRP direct a ribosome to the ER membrane

44
Q

Start and stop signals

A

Start and stop signals determine the arrangements of a transmembrane protein in the lipid bilayer

Signal sequence- trigger the opening of the pore in the protein translocator

45
Q

Single pass transmembrane

A

A single pass Tran protein is retained in the lipid bilayer

46
Q

Double pass transmembrane

A

A double pass transmembrane protein has an internal ER signal sequence

47
Q

Unfolded protein respon UPR

A

Misfolded proteins in the ER activate an unfolded protein response

Chaperones prevent misfolded pr partially assembled proteins from leaving the ER

48
Q

ER induced stress in inflammation

A

Affect pancreatic beta cells as well as adipocytes and macrophages
Cancer cystic fibrosis

49
Q

Environmental or genetic factors of ER stress

A

Proteins folding incorrectly

Alzheimer
Parkinson 
Cancer
Obesity 
Diabetes
50
Q

Golgi Apparatus sides

A

Cis - facing to ER

Trans - facing to membrane

51
Q

Function of golgi

A

Lipid biosynthesis and maturation (sphingolipin)
Carbohydrate synthesis and o linked glycosylation
Formation of secretary vesicles and secretion
Sulfation(give neg charge-> interaction with other…)
Addition of mannose6phosohate to lysosomal protein(with them can go to lysosome)
Storage of protein lipoid material

52
Q

Glycosylation

A

Proteins and lipids are further modified by mostly glycosylations in the Golgi apparatus

53
Q

Lysosome

A

Contains a large variety of hydrolytic enzymes, which are only active under acidic conditions

H pumps make the inside of the lysosome acidic 5.0

Materials destined for degradation in lysosomes follow different pathways to the lysosome

!autophagy!= degradations for obsolete parts of the cell- the cell literally eats itself

54
Q

Lysosomal storage Diseases

A

No digestion => storage!

Fabry disease 
Gaucher disease
Mucopolysaccharidosis
Niemann pick c disease 
Tay sachs diseases 
Metachromatic leukodystrophy and Krabbe disease
55
Q

Life cycle of M.tuberculosis

A

Inhaled by aerosols
Transmitted to the lungs
Phagocytozed by macrophages
Apoptosis

56
Q

Vesicular Transport Nobel price

A

James rothman, randy schekman, Thomas Sudhoff have discovered the molecular principles that govern how this cargo is delivered to the right place at the right time in the cell

57
Q

Vesicular transport

A

Distrubances in this system have deleterious effects and contribute to conditions such as neurological diseases, diabetes and immunological disorders

58
Q

Vesicle budding and fusion

A

Occur during vesicular transport

Budding vesicle with contents selected for transport

59
Q

Function

A

Carry soluble proteins and membrane between compartments
Bud from one membrane and dude with another carry membrane components and soluble proteins between compartments of the endomembrane system and the plasma membrane

60
Q

Exocytosis

A

Delivery of newly synthesized proteins, lipid and carbohydrates to either plasma membrane or extracellular space

61
Q

Endocytosis

A

Removal of plasma membrane components, capture important nutrients deliver them to the internal compartment