Topic 3 - Cell Biology Flashcards

(77 cards)

1
Q

Treadmilling

A

when polymer formation reaches a steady state, subunits undergo a net assembly at the plus end and a new disassembly at the minus end at an identical rate. The polymer maintains a constant length, even though there is a net flux of subunits through the polymer

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2
Q

Cofilin

A

binds ADP-actin filaments and promotes disassembly

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3
Q

Profilin

A

binds G-actin monomers and promotes the addition of these to growing filaments. This also prevents nucleation

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4
Q

ion-channel-coupled receptors

A

also called transmitter-gated ion channels or ionotropic receptors - involved in rapid signalling between neurons and other electrically excitable target cells

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5
Q

G-protein-coupled receptors

A

activation leads to formation of an activated receptor and G-protein complex which further activates the G-protein and associated enzymes

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6
Q

enzyme-coupled receptors

A

many have intrinsic enzymatic activity, many others rely on associated enzymes. Signal molecules activate most enzyme-coupled receptors by promoting their dimerisation, which results in the interaction and activation of the cytoplasmic domains

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7
Q

Cotranslational translocation

A

if ribosomes are ER bound, proteins will be simultaneously translated and translocated

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8
Q

post-translational translocation

A

proteins on free ribosomes are first translated and then translocated

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9
Q

proteoglycans

A

form the ‘ground substance’ which resists compression and allows diffusion through the ECM

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10
Q

fibrous proteins

A

(collagen and elastin) provide strength, organisation and resilience to the ECM

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11
Q

glycoproteins

A

help with adhesion and support the cells within the ECM

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12
Q

Glycosaminoglycans (GAGs)

A

long, unbranched polysaccharides found in the extracellular matrix of connective tissues, including skin and cartilage. They are known for their ability to bind and retain water, contributing to tissue hydration and physical properties like elasticity and support

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13
Q

hyaluronan

A

acts as a space filler during tissue morphogenesis and repair

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14
Q

collagen

A

the major protein in ECM (25% of protein mass in animals). Cross-linking affects tensile strength. After secretion, covalent bonds (between lysine residues) cross-link the collagen molecules, particularly in non-helical ends. The extent of cross-linking affects tensile strength: inhibition of cross-linking reduces tensile strength, the highest level of cross-linking occurs in tendon collagen and provides the highest tensile strength

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15
Q

elastin

A

provides elasticity to tissues - It’s a crucial component of the body’s connective tissues, particularly in areas where flexibility is essential, such as the skin, lungs, and blood vessels. Elastin helps these tissues return to their original shape after being stretched or compressed

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16
Q

fibronectin

A

Fibronectin is a high-molecular-weight glycoprotein found in the extracellular matrix (ECM) of animal and human tissues. It acts as a key bridge between the ECM and cells, facilitating cell adhesion, migration, and differentiation.

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17
Q

basement membrane / basal lamina

A

specialised form of ECM. Epithelial cells produce the basement membrane upon which epithelial cells sit. A basement membrane also surrounds muscle cells, fat cells and Schwann cells

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18
Q

Describe how “inside-out” and “outside-in” integrin signalling regulates focal adhesion structure

A

Internal activation of integrin receptors. Interaction of integrins with ECM proteins. Recruitment of intracellular adaptors and kinases and interaction with cytoskeleton

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19
Q

The cytoskeleton

A

composed of intracellular structures, polymers that form an interlinked network. This network is important for cell shape, movement, division, trafficking

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20
Q

Actin filaments (microfilaments)

A

essential structural components of the cytoskeleton, playing a crucial role in cell shape, movement, and division. Helical polymers of the protein actin. G-actin (monomeric) and F-actin (filamentous). Helical, flexible, dynamic structures, 8nm diameter. Organise into linear bundles, 2D networks and 3D gels

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21
Q

Microtubules

A

long, hollow cylinders made of the protein tubulin. With an outer diameter of 25nm, they are much more rigid than actin filaments. They are long and straight and frequently have one end attached to a microtubule-organising center called a centrosome

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22
Q

Intermediate filaments

A

rope-like fibers with a diameter of about 10nm; they are made of intermediate filament proteins. One type of intermediate filament forms a meshwork called the nuclear lamina just beneath the inner nuclear membrane. Other types extend across the cytoplasm, giving cells mechanical strength. In epithelial tissue, they span the cytoplasm from one cell-cell junction to another, strengthening the entire epithelium

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23
Q

Arp2/3 complex

A

promotes filament branching

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24
Q

nucleation

A

a helical polymer is stabilised by multiple contacts between adjacent subunits. In the case of actin, two actin molecules bind relatively weakly to each other, but addition of a third actin monomer to form a trimer makes the entire group more stable. Further monomer addition can take place onto this trimer, which therefore acts as a ‘nucleus’ for polymerisation. The assembly is relatively slow, which explains the lag phase seen during polymerisation. The lag phase can be reduced or abolished by adding premade nuclei.

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25
ATP and GTP caps
the rate of addition of subunits to a growing actin filament or microtubule can be faster than the rate at which their bound nucleotide is hydrolysed. Under these conditions, the end has a 'cap' of subunits containing the nucleoside triphosphate, ATP cap on actin filament or a GTP cap on a microtubule
26
mesenchymal cell migration
focal adhesions from behind protruding lamellipodia that connect to contractile stress fibers, bracing the cell against the surface (substratum) across which it is migrating
27
dynamic instablility
microtubules depolymerise about 100 times faster from an end containing GDP-tubulin than from one containing GTP-tubulin. A GTP cap favours growth, but if its lost, depolymerisation continues. Individual microtubules can therefore alternate between a period of growth and a period of rapid disassembly, a phenomenon called dynamic instability
28
kinesin
transports the plus-end of microtubules
29
dynein
transports towards the minus-end of microtubules
30
similarities and differences between kinesin and dynein
both move along microtubules, kinesin to plus-end, dynein to minus-end. Both engage with cargo. Kinesin typically does this via light chain (more direct), while dynein binds via another protein complex (dynactin). Both use ATP to fuel their movements. Dynein typically moves faster than kinesin
31
epithelial tissue, what do they line and form?
cells are intimately connected to each other (junctions between cells), cells have apico-basal polarity, the tissue has little ECM (just basement membrane). Mechanical stresses are transmitted from cell to cell by cytoskeletal filaments, anchored to cell-matrix and cell-cell adhesion sites. Line external body surfaces, internal body cavities, tube organs that communicate with the exterior (e.g. digestive). Epithelial tissues form secretory parts of glands and their ducts, receptors for certain sensory organs, and the brain
32
connective tissue
cells have few contacts with each other, cells have no apico-basal polarity, tissues have a large amount of ECM. ECM directly bears mechanical stresses of tension and compression
33
Apico-basal polarity
the apical and basal membranes of epithelia often have different structures and properties. Apical: absorption, secretion, membrane specialisations (e.g. microvilli, cilia). Basal: adhesion to ECM, secretion into sub-mucosa.
34
Functions of epithelial tissues
different types have different functions; protection from mechanical, abrasive and environmental stresses, waterproofing, thermoregulation, absorption or secretion
35
tight junction
seals the gap between epithelial cells. acts as a barrier, regulating the movement of substances between cells and also maintaining cell polarity. They form a seal between cells, preventing the leakage of fluid and solutes through the space between them, while also preventing the movement of proteins and lipids between the apical and basolateral membrane domains.
36
adherens junction
connects actin filament bundle in one cell with that in the next cell
37
desmosome
connects intermediate filaments in one cell to those in the next cell
38
gap junction
allows the passage of small water-soluble molecules from cell to cell
39
actin-linked cell-matrix junction
anchors actin filaments in cell to extracellular matrix
40
hemidesmosome
anchors intermediate filaments in cell to extracellular matrix
41
What are the key concepts of translocation into the mitochondria?
An N-terminal signal sequence on the protein to be translocated is recognised by TOM receptor complex. The protein is threaded through TOM and TIM translocation channels. The outer and inner channels align and the protein is threaded into the mitochondrial matrix. A signal peptidase cleaves off the signal sequence. ATP drives the transport, 'pulling' the protein through TIM complex.
42
Ran-GEFs
localised to the nucleus (bound to chromatin). They exchange GDP for GTP. There's a high concentration of Ran-GTP in the nucleus, so it wants to move back to the cytosol (down concentration gradient), which drives the return of empty importin to the cytosol
43
Ran-GAPs
Localised to the cytosol. Ran-GTP hydrolysed to Ran-GDP. Ran-GDP dissociates from importins (and is carried back to the nucleus). The empty importin can pick up cargo or return to the nucleus empty.
44
What are the key concepts of nuclear transport?
The nuclear pore complex (NPC) drives the import/export of proteins. A signal sequence in a protein determines whether it's imported or exported and is recognised by nuclear import (importins) or export receptors (exportins). The GTPase cycle drives import and export. Nuclear import and export receptors change their conformation and are recognised by the NPC.
45
The secretory pathway
Protein molecules are transported from the endoplasmic reticulum to the plasma membrane or (via endosomes) to lysosomes
46
The endocytic pathway
Molecules are ingested in endocytic vesicles derived from the plasma membrane and delivered to early endosomes and then to lysosomes.
47
Autophagy
cytoplasmic components engulfed into an autophagosome are delivered to lysosomes.
48
Retrieval pathways
Many endocytosed molecules are retrieved from early endosomes and are returned to the cell surface for reuse; some molecules are retrieved from early and late endosomes and returned to the Golgi apparatus and some are retrieved from the Golgi and returned to the ER
49
Clathrin coat protein
mediates transport from the plasma membrane via endocytosis and transport from the golgi and endosomes
50
COPII
facilitates forward ER to golgi transport
51
COPI
facilitates reverse golgi to ER transport
52
retromer
facilitates transport from endosomes to golgi apparatus
53
How is the specific identity of the various vesicles controlled between the endocytic, secretory and retrieval pathways?
Different vesicle coat proteins (clathrin, COPI and COPII) are used to regulate vesicle formation in specific compartments. Different Rab proteins are displayed on specific organelle membranes, regulating vesicle transport. V-SNAREs (transport vesicles) and t-SNAREs (target membrane) are expressed on specific organelle membranes and regulate vesicle fusion.
54
How is the clathrin coat assembled and disassembled?
Cargo has been placed into the cargo receptors, which triggers the clathrin to come over. The assembly of the coat introduces curvature into the membrane, which leads to the formation of a coated bud. The adaptor proteins on the cytosolic side of the membrane bind both clathrin triskelions and membrane-bound cargo receptors, allowing them into the vesicle. Further bending of the membrane and fission proteins recruited to the neck of the budding vesicle. The coat is rapidly lost after the vesicle buds off.
55
COPII coat formation
Cargo receptor + cargo + coat-recruitment GTPases + adaptor proteins + coat proteins = vesicle formation
56
Vesicular tubular clusters
Move along microtubules to carry proteins from the ER to the Golgi apparatus. COPI coats mediate the budding of vesicles that return to the ER from these clusters (and from the Golgi apparatus)
57
What are the common steps in vesicle coating?
Small GTPase (molecular switch) gets activated (a GEF exchanges GDP for GTP). Activated GTPase associates with the membrane and recruits adaptor proteins. Adaptor proteins recognise cargo and cause a slight curvature of the membrane. Coat proteins are recruited to encage the vesicle. Vesicle is pinched off by protein activities and/or through membrane fusion/fission. The coat is usually shed off the vesicle by GTPase activity.
58
What happens in the Golgi apparatus?
Protein modification and protein sorting occur, directing vesicles to locations including lysosomes, the plasma membrane and secretory vesicles.
59
Signal-mediated diversion to lysosomes (via endosomes)
Proteins with mannose 6-phosphate (M6P) marker are diverted to lysosomes (via endosomes) in clathrin-coated transport vesicles.
60
What are the two key processes required for RTK activation?
receptor dimerisation and phosphorylation
61
Ras GTPases are common intracellular relays of RTK signalling. So how does Ras relay the RTK signal?
1. An activated RTK binds to an adaptor protein 2. The adaptor protein binds a GEF, e.g. Sos (guanine nucleotide exchange factor) 3. Sos activates Ras by exchanging GDP for GTP
62
M-Cdk
The cyclin-Cdk complex that stimulates entry into mitosis at the G2/M checkpoint
63
cyclin
protein whose concentration rises and falls during the eukaryotic cell cycle
64
Cdk
a protein kinase that must be complexed with a cyclin protein to act
65
Cyclin-Cdk complex
protein assembly that forms periodically during the cell cycle as cyclin levels increase
66
Start G1/S transition
enter cell cycle and proceed to S phase
67
G2/M transition
enter mitosis
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Metaphase-to-anaphase (spindle) transition
trigger anaphase and proceed to cytokinesis
69
APC/C (anaphase-promoting complex)
The primary control factor in the metaphase-to-anaphase transition. Marks certain proteins for rapid degradation (M-cyclins, S-cyclins) and triggers breakdown of the Cohesin complex which is the key component holding sister chromatids together
70
Mitogens
An extracellular signal that stimulates cell division. Trigger re-entry into the cell cycle.
71
Growth factors
An extracellular signal that stimulates cell growth
72
Survival factors
An extracellular signal that promotes cell survival by suppressing cell death by apoptosis. In many cell types apoptosis is the default state, therefore some cells require survival factors to survive.
73
Rho
A member of the Rho GTPase family that controls the formation of stress fibres and focal adhesions in actin cytoskeleton organisation
74
Rac
A member of the Rho GTPase family that regulates the formation of lamellipodia and membrane ruffles
75
Myosin
A motor protein that moves along actin filaments using the energy from ATP hydrolysis to generate force and movement. It plays a crucial role in muscle contraction and a wide range of other cellular processes
76
nervous tissue
specialised to facilitate electrochemical signalling
77
What are the types of epithelia?
Stratified (in layers), squamous (flattened), columnar (like columns), cuboidal (cube shaped)