Module 2 Vocab Flashcards
Lipid Bilayer
The membrane structure of the plasma membrane in a cell, ~ 5 nm thick
Phopholipids
The basic component of the plasma membrane, is amphipathic witha hydrophillic head and hydrophobic tail
Fluid mosaic model
Membrane model which suggests that proteins and lipids can move freely laterally in the membrane
Membrane fluidity
Determines the ability of particles to move about in a membrane laterally
FRAP
Fluorescence recovery after photobleaching; used to study membrane protein diffusion
SPT
Single particle tracking microscopy; tracks the movement of a particel tagged with a gold flake
Integral membrane proteins
Includes transmembrane, monolayer-associated, and lipid-linked proteins; proteins that are embedded into the membrane directly
Peripheral Membrane Proteins
Only includes rotein attached proteins; proteins indirectly bound to the membrane
Transmembrane domain
Portions of a protein that tend to form alpha helices with hydrophobic side chains, allowing them to span the membrane favorably
Passive Transport
Transport through a cell that happens without the addition of energy
Active Transport
Transport through a cell that requires teh addition of an energy source
Diffusion
A form of passive transport that uses concentration gradients to move molecules
Facilitated Diffusion
Passive transport of molecules through a channel in the membrane
Rate of diffusion across a membrane
Dependent on molecule size, charge, solubility, membrane viscosity, concentration gradient, receptor/channel protein density, and cell temperature
Osmosis
Movement of water from low to high solute concentration
Isotonic
Concentration equilibrium or maintained
Hypotonic
Dilute solution
Hypertonic
Highly concentrated solution
Coupled Transporter
Active transport method that moves a type of molecule out of the cell and at least one different molecule into the cell
ATP-Driven pump
Uses ATP as an energy source to transport molecules against their concentration gradient into or out of a cell
Light-driven pump
Uses energy from light to drive molecules against their electrochemical gradient
Uniporter
Transports one molecule in one direction
Symport
A type of coupled transport that co-transports different molecules
Antiport
A type of coupled transporter that transport one molecule in and one out
Coupled Transporter
Exploit the energy stored in electrochemical gradients of one solute to drive the pumping of another solute against its gradient
ABC Transporters
ATP binding cassette transporters; use the energy of ATP hydrolysis to switch conformations
Signal Sequences (SS)
20-22 amino acid sequences located mostly at the N-terminus of proteins with a long hydrophoic stretch followed by a charged amino acid; indicates where a protein goes in the cell
Smooth endoplasmic reticulum (SER)
Synthesizes and secretes hormones, detoxifies organic compounds
Sarcoplasmic reticulum
SER in muscle cells that stores and releases Ca++
Rough Endoplasmic
Site of synthesis of specific proteins
Co-Translational Translocation
Protein enters the ER as it is being synthesized
Post-Translational Translocation
Proteins that enter the ER after they are synthesized
Translocator Protein
A protein that binds to the signal sequence of a growing soluble protein and deposits it into the ER
Signal Peptidase
Cleaves the signal sequence of a protein following its translocation into the ER
Signal Recognition Particle (SRP)
A complex of 6 polypeptides and 1 cytoplasmic RNA that binds to the signal sequence; when bound to the SS temporarily halts translation
SRP Receptor
Binds to the SRP and allows the SS to complex with the protein translocator
N-terminus
The terminus of the protein that faces the inside of the ER lumen
Transmembrane Proteins
Proteins that span across the plasma membrane of a cell or organelle; part of their protein is in the cytoplasm, part in ER lumen during synthesis (N-terminus)
STOP Transfer Sequence
Transmembrane domains of proteins that halt their movement through a membrane during synthesis
Hydropathy Plot
A plot that shows the number of transmembrane domains in a protein
Disulfide Bonds
Proteins that are transported to the ER have them as the environment inside is oxidizing
Protein Disulfide Isomerase
Facilitate the formation of S-S bonds and can correct errors
Chaperone Proteins
Help to correctly fold proteins during and after synthesis
Self-fold
Proteins do this due to interactions between amino acid side chains and their surrounding medium
Aggregates
Incorrectly folded proteins that are not proteolyzed grouped together; can be broken down by autophagocytosis
Autophagocytosis
A recycling mechanism in the cell
Ubiquitin
A sugar that is added to proteins to signal them for degradatino in the proteosome
Proteasome
A small vesicle link organelle responsible for protein degradation
Proteasome Mediated Degradation
An energy requiring process that recognizes ubiquitin sugar as a signal for degradation
Sugar Addition and Modification
Occurs in the ER and Golgi and is helpful in determining topology of membrane proteins in membranes, serves as binding sites, helps secreted and membrane proteins to fold, and protects membrane proteins from attack by proteases
Exocytosis
The process of transporting proteins and other cargo out of the cell; for proteins it goes from the ER to the Golgi and outward from there to the plasma membrane and is released from the cell
Golgi Body
Discovered by Camillo Golgi; modifies proteins by the sequential addition and removal of sugars and other post-translational modifications
Golgi Stack
Comprised of the cis Golgi network (closest to ER), the cis cisterna, the medial cisterna, the trans cisterna, and the trans Golgi network
Cis Glogi Network
Responsible for sorting proteins and for the phosporylation of oligosaccharides on lysosomal proteins
cis cisterna
Responsible for the removal mannose sugars (Man)
medial cisterna
Responsible for the removal an mannose sugars and the addition of N-Acetylglucosamine (GlcNAc)
trans cisterna
Responsible for the addition of Galactose sugars (Gal) and NANA
trans Golgi Network
Responsible for sorting, the suflation of tyrosines and carbohydrates, and sending proteins to their next location
Nuclear Pore Complex (NPC)
Responsible for transport of cargo into and out of the nucleus; 50-100 protein complex, with fibrils on the cytosol side, a basket inside, is a ring shape with 8-fold symmetry
Nuclear Pore
Molecules 60kD and smaller can diffuse through, but larger marcomolecules (larger proteins, RNA, and Ribosomes) must be transported through; proteins can be transported folded or unfolded
Nuclear transport
Directed by nuclear pores and associated with regulatory proteins
Nuclear Import
The import protein binds to NLS and passes through the NPC with Ran-GDP, then releases the protein and binds to Ran GTP to passes back through the NPC
Nuclear Localization Sequence
A short stretch of amino acids the mediates the transport of nuclear proteins into the nucleus
Ran GTPase
Most abundant small GTPase in the cell and functions as a molecular switch by converting between the active GTP and inactive GDP-bound conformations
Nuclear Export
Export protein beinds the NES and Ran-GTP to pass through the NPC, releases both then passes back through the NPC
Green Fluorescent Protein (GFP)
A protein isolated from the Crystal Jellyfish Aqueora victoria; allows for the creation of fusion proteins to allow the identification of organelles or the tracking of proteins and protein activity in real time
Fusion cDNA
To make this you fuse the sequence corresponding to the C-terminus of a selected protein with the N-terminus of the GFP making sure to maintain both reading frames and removing the selected proteins stop codon while retaining GFP’s
Restriction Enzymes
Proteins that cut specific sequences of nucleotides in dsDNA, can create sticky or blunt ends
Sticky Ends
Allow for fusion of the ends of DNA sequences by making exposed nucleotides; —|,,, ‘’’|—
Blunt Ends
Prevents fusion of the ends of DNA sequences; —| |—
Mitochondrial Matrix
Site of folding for mitochondrial proteins; surrounding by the inner mitochondiral membrane
Mitochondria
“Power house of the cell lol”; an organelle with an outer plasma membrane and an inner membrane, with cytosol filling the intermembrane space
Precusor Proteins
Unfolded proteins that are transported through the cytosol to the mitochondria
Mitochondrial protein trafficking
Unfolded proteins are bound by their signal sequence to protein translocator in outer membrane, once the protein has begun to pass through a second protein translocater located on the inner membrane will bind to the signal sequence and transport the protein into the matrix
Peroxisome
Responsible for digesting toxins and synthesizing phospholipids; most of its proteins are translocated from cytosol with a tripeptide signal sequence (Ser–Lys-Leu)
Zellwager Syndrome
Caused by mutations in genes that encode peroxisomal “import” protein; autosomal recessive
Endosome
Plays a central role in vesicular transport into and out of cells
Coated Vesicles
Vesicles with a coat of distinctive coat protiens; coat is shed once the vesicles buds from parent organ or cell structure
Coat Proteins
Give shape to vesicles, recognize cargo proteins, and form specialized membrane patches/pits before budding
Clathrin-coated Vesicles A
Originate in the Golgi apparatus and go to lysosomes via endosomes, coated with clathrin and adaptin 1
Clathrin-coated Vesicles B
Originate at the plasma membrane and go to the endosomes, coated with clathrin and adaptin 2
COPII-coated Vesicles
Originate in the ER and go to the Golgi cisterna, coated in COPII proteins
COPI-coated vesicles
Originate in the Golgi cisterna and go to the ER, coated with COPI protein
Clathrin triskelion
Made of 3 clathrin subunits with the N-termini turning inwards; forms a sort of basket
Adaptins
Proteins that bind clathrin to membranes by contacting the inner shell of the clathrin triskelion
Invagination of Plasma membrane
Drive by the strucutre of clathrin allowing it to mediate endocytosis
Dynamin
A GTPase that facilitates the budding off of clathrin coated vesicles via constriction; causes GTP hydrolysis
LDL
Low-density lipoproteins; responsible for the transport of cholesterol (the bad cholesterol?)
Transcytosis
Endocytosis followed by exocytosis, permits movement of large molecules across epithelia
Rab-tethering protein
Binds to the exterior of vesicle and helps to direct recognition of the vesicle by the destination organelle
SNARE Proteins
A transmembrane protein that interfaces with a different version of itself to catalyze the fusion of the vesicle membrane with the organelle membrane
Botox
Forces muscle contraction by blocking Ca2++ channels in nerves
Endocytosis
Plasma membrane invagination that forms vesicles that bud off into the cytoplasm
Pinocytosis
Non-specific endocytosis of fluids and small molecules
Phagocytosis
Actin and receptor mediated endocytosis of large particulates and bacteria
Autophagy
Use of endocytic compartments to recycle cytosolic proteins and organelles
Lysosome
The result of a vesicle containing hydrolases fusing with an endosome; membrane bound sacs of at least 50 hydrolytic enzymes that digest both extracellular matter and intracellular decayed organelles; work at pH of 4.6 maintained by proton pump
Lysosomal Proteins
Marked by glycosylation in the ER with mannos-6-phosphate sugar and are transported to the trans Golgi network to be transported to lysosomes
Tay Sachs disease
Lysosomal storage disease resulting from beta-N-hexosamindase A deficiency, causes GM2 buildup in bloated lysosomes
Cystic Fibrosis Transmembrane Protein (CFTR)
Impair transport of CFTR protein from ER to plasma membrane, decreasing its prevalence slowing the transport of Cl- across plasma membrane resulting in pulmonary mucous thickening
Exosomes
Extracellular vesicles produced from multivesicular bodies; they are specialized endosomes that contain membrane-bound intraluminal vesicles