Cellular Organization and Function (Cooper, Geoffrey M. 2000. The Cell, A Molecular Approach, 2nd Edition-Chapter 1, p. 3-15; Ch. 10, p. 389)
A. General functions of parts of the cell--cell membrane, endoplasmic reticulum, Golgi, lysosomes, peroxisomes, cytoskeleton, mitochondria, chloroplasts, vacuole
B. Differences-plant vs animal cells
C. Distinguishing characteristics, differences--prokaryotes, eukaryotes
D. Origin of membrane systems (ER, nuclear membrane)
E. Origin of mitochondria, chloroplasts-from endosymbiotic bacteria

Gene Regulation--Control of Gene Expression
Multiple levels of gene expression and regulation
I. Pre-transcriptional control
A. X chromosome inactivation--(Ch. 8, p. 327-328)
Description of the process, inactive X appears as Barr body, inactive X passed on to progeny cells (eg., coat color genes), not all genes on inactive X are inactive, reactivation of inactive X during oogenesis, mechanism of X chromosome inactivation

B. Selective amplification of genes
1. Programmed amplification--amplification of genes for rRNA during oogenesis-- (Ch. 5, p. 221-222) Description of the process, amplified genes packaged into many nucleoli, "purpose" of amplification
2. Unprogrammed amplification of oncogenes leading to uncontrolled growth àtumors (Ch. 15, p. 622-635) Definition of oncogenes, proto-oncogenes, functions of proteins coded by oncogenes/proto-oncogenes (oncoproteins), examples of cancers where oncogene amplification occurs, what happens to the "extra" genes

C. Translocation of segments of chromosomes leading to the development of cancers (Ch. 15, p. 629-630) what happens during chromosomal translocation, description of an example of chronic myelogenous leukemia, how the translocation leads to the development of the cancer

D. Rearrangement of DNA to produce antibody genes (Ch. 5, p. 211-215) Structure of antibody proteins, how the DNA rearrangement occur-V-J joining to produce light chain genes, V-D-J joining to produce heavy chain genes, how the DNA in between is removed (sequences after V segment and before J segment are complementary and form loop), significance of DNA rearrangement in production of antibody genes

Immune System function: Activation of B cells to produce antibodies (Handouts)-Steps leading to activation of B cells, including uptake of antigens (eg., viruses, bacteria) by macrophages, breakdown of antigens within macrophages, antigen fragments combine with MHC (major histocompatability complex) proteins and integrate into the membrane, antigen-MHC recognized by T cell receptor proteins on surface of T cells, interaction of macrophage with T cell activates T cell to divide, T cell interacts with B cell, activating the B cells to divide and differentiate into antibody-secreting cells.

Gene Regulation: Transcriptional Control in Prokaryotes
Overview of process of transcription (Ch. 6, p. 227-231)
General steps of transcription-binding of RNA to promoter region, localized unwinding of the DNA, initiation of RNA synthesis initiation, elongation, termination
Transcription in prokaryotes
Role of sigma subunit of RNA polymerase
Process of elongation in transcription
Prokaryotic promoter sequences-sequences to which RNA polymerase binds
Pribnow (or TATA) box at -10; -35 sequence
Termination of transcription-formation of stem loop structure of transcribed RNA slows down RNA polymerase; As of DNA transcribed as Us of RNA; formation of stem-loop and weak A-U interaction causes RNA to dissociate from the DNA (and 2 strands of DNA
re-associate)

Regulation of Transcription in Prokaryotes -- (Ch. 6, p. 231-234)
Definition of an operon
Regulation of transcription of genes of lactose (lac) operon, an inducible operon
Sequences of DNA of lac operon and their functions-regulatory gene (lac I gene), promoter, operator, structural genes (lac Z, lac Y, lac A)
Explain regulation of transcription of the lac operon when lactose is absent, and when lactose is present-how does lactose allow transcription of the genes coding for enzymes to break down lactose?
Role of cAMP binding to CRP (cAMP receptor protein, also known as CAP-catabolic activator protein). How does the cAMP-CRP complex stimulate transcription?
Relationship of glucose levels to levels of cAMP
Explain how to obtain maximum synthesis of the lac operon-the role of lactose, the lactose repressor, cAMP-CRP complex, and glucose

Regulation of the tryptophan (trp) operon, a repressible operon
Genes code for enzymes to synthesize tryptophan, an amino acid
Explain regulation of transcription of the trp operon when tryptophan is absent, and when tryptophan is present-how (and why) does the presence of tryptophan block transcription of the genes coding for enzymes to synthesize tryptophan?
Comparison of regulation of lac operon and regulation of trp operon

Comparison of gene organization and regulation in prokaryotes and eukaryotes -differences in function (purpose) of gene regulation; organization of genes; number of RNA polymerases; transcription-translation coupled in prokaryotes, processes in separate compartments in eukaryotes; regulation primarily transcriptional in prokaryotes, many levels of regulation in eukaryotes; RNA processing (splicing) in eukaryotes, RNA does not require processing in prokaryotes; in eukaryotes, DNA packaged with histone proteins to form chromatin, prokaryotes-no protein associated-naked DNA; also differences in composition of ribosomes and translation factors.

Regulation of Transcription in Eukaryotes (Ch. 6, p. 236-253)
DNA sequences to which RNA polymerase II and transcription factors (TFs) bind
Characteristics of enhancer elements (DNA sequences)
A group of general TFs bind to TATA box and allow RNA polymerase II to bind
Many gene activator proteins interact to initiate transcription-gene-specific and general TFs
Interaction of TFs close to start with TFs bound to distant sequences (eg. enhancer sequences)-activator proteins (TFs) bind enhancers, architectural proteins bend DNA, co-activator proteins bind activators and general TFs at TATA box-relay signal from activators
How steroid hormones activate transcription

Modification of chromatin structure before transcription
Structure of chromatin, chromosomes--(Ch. 4, p. 146-150)
nucleosome, solenoid (30 nm fiber),
steps in formation of metaphase chromosome

Methods to "loosen" chromatin structure and expose gene for transcription --
(Ch. 6, p. 253-256)--removal of H1 histone à unfold solenoid (30 nm fiber) to nucleosome (10 nm fiber); binding of hormone-receptor complex (as activator) to specific DNA sequence (enhancer sequence called response element); activator recruits co-activator which has acetyl transferase activity-co-activator adds acetyl groups to histones and loosens interaction of histones with DNA-histones are removed in the region of the TATA box to allow TFs and RNA polymerase to bind and start transcription;
Once the RNA polymerase is bound, the enzyme can transcribe through ("around") the nucleosomes covering the rest of the gene-as RNA polymerase approaches a nucleosome, the DNA spools out; the DNA that has been transcribes wraps around the histone core forming a loop-as more and more DNA is unspooled and the DNA behind the RNA polymerase spools around the histone core, the nucleosome ends up behind the RNA polymerase

Transcriptional control in development (Ch 6, p. 248-249)
Genes which control anterior-posterior polarity, establish body plan and segmentation are turned on in sequence--proteins produced at one stage act as TF to stimulate development of the next stage; similar genes found in fruit flies and mice (mammals)

Post-transcriptional control
Processing of RNA transcript-- (Ch. 6, 257-265)
Addition of "cap" sequence to 5' end (what is the sequence of the "cap"--it is derived from what nucleotide?)
Addition of poly A to 3' end (how is poly A added?)
Removal of introns, splicing together of exons--Explain the lariat model for removal of introns, splicing of exons; What are "snurps"? -What is the role of "snurps" in RNA splicing? How do the snRNAs interact with the pre-mRNA?
Exons code for protein domains
Alternative RNA splicing-- (Ch. 6, p. 265-266)
What does "alternative RNA splicing" mean? Explain examples. What mechanisms control alternative RNA splicing?-repressor blocks splicing, or activator initiates splicing

Translational Control
Overview of Translation (Ch. 7, p. 273-287)
Amino acid activation--attachment of amino acid to its tRNA--how occurs
Formation of initiation complex in process of translation
Steps of elongation and termination of translation
Structure of transfer RNA, ribosomal RNA
Structure of prokaryotic, eukaryotic ribosomes
relative size (prok vs. euk), types of rRNAs, relative number of proteins

Control at the level of translation
Changes in stability (half-life) of mRNA-regulation of degradation of mRNA
(Ch 6, p. 267-268)
Examples of systems that have regulation of mRNA stability,
Mechanisms to regulate life span of mRNA-example of transferrin receptor mRNA whose degradation is regulated by an iron-binding protein
Regulation of initiation of translation by a specific protein-(Ch 7, p. 288-290)-example of regulation of ferritin mRNA translation initiation by iron-binding protein
Regulation of protein degradation-(Ch. 7, p. 305-307)-binding of ubiquinating enzyme complex to targeted proteins, attachment of ubiquitin molecules to target protein, binding of target protein-ubiquitin complex to proteasome, target protein degraded by proteases of proteasome; structure of proteasome

Membrane Structure (Ch. 2, p. 79-84; Ch. 12, p. 467-476)
General functions of membranes
Overall structure of membrane
Membrane Lipids--(Ch. 2, p. 44-47)
Structure of phospholipids--2 fatty acids (one unsaturated), glycerol, head end --phosphate linked to head group such as choline
Spingolipids--structure
Glycolipids--structure, location in membrane
Gangliosides--general structure
Cholesterol--proportion of membrane, structure, interaction with other lipids in membrane
Asymmetry of lipids in membrane--what it means
Lipid mobility (membrane fluidity)--role of cholesterol, role of temperature--gel -> fluid transition, types of lipids which maintain fluidity, types of movements of lipids
Explain the role of cholesterol in maintaining membrane fluidity

Membrane Proteins--(Ch. 2, p. 50-56)
Gel electrophoresis (Ch. 3, p. 106-107)-separates proteins based on size, shape, charge, or isoelectric point--slab gel formed between 2 glass plates(SDS-polyacrylamide gel electrophoresis), or pH gel in tubes (isoelectric focusing); SDS-polyacrylamide gel electrophoresis separates proteins by size because SDS gives proteins constant shape and charge;
2-dimensional gel electrophoresis separates proteins by isoelectric point (1st dimension) and size (2nd dimension)
Membrane Proteins--(Ch. 2, p. 50-56; Ch. 12, p. 470-476)
Interactions of integral (transmembrane) proteins with bilayer--single alpha helix, multiple alpha helices
Interactions of peripheral proteins with membrane-
Lipid-anchored proteins--through fatty acid chain, oligosaccharide link
Glycoproteins--define, structure, functions
Mobility of membrane proteins-types of movements of membrane proteins, how cell fusion
experiment showed lateral diffusion

Protein Sorting, Distribution, and Secretion; Exocytosis and Endocytosis

Intracellular sorting of proteins (Ch. 9, p. 347-372)
Protein synthesis begins on ribosomes in cytoplasm; for some proteins, translation completed in cytoplasm, and proteins may be imported into organelles such as the nucleus, mitochondria, chloroplasts, peroxisome; for other proteins, protein synthesis continues into ER lumen, proteins transported through Golgi, then to destinations including secretory vesicles, lysosomes, and cell membrane.
Types of proteins synthesized on free ribosomes; types of proteins synthesized on ribosomes bound to endoplasmic reticulum

Signals directing proteins to destinations within the cell are built into proteins (coded by DNA sequence in gene)-called signal sequences, signal peptides, target sequences, leader sequences, signal patches

Co-translational Import of Proteins into ER
Explain how a protein is transferred across the membrane of the ER--the co-translational transfer of protein. Include the role of the signal sequence (signal peptide), signal recognition particle (SRP), SRP receptor, translocon (also called the pore protein, protein-translocating channel, translocator protein), GTP, cleavage of signal sequence by signal peptidase
Structure of the signal-recognition particle (SRP)
Protein folding in the ER-role of chaperone proteins

Glycosylation-In N-linked glycosylation, a 14-sugar core oligosaccharide (2 N-acetylglucosamine, 9 mannose, 3 glucose) is linked to dolichol phosphate, a lipids embedded within the ER membrane. As the protein is being translated into the ER, the sugars are transferred as a group to asparagine amino acids of the newly forming polypeptide. In most proteins the oligosaccharide unit is modified (some sugars removed, some added) as the protein moves through the ER and Golgi.
Functions of sugar groups-

Other protein modifications occur as the protein moves through the ER and Golgi complex-
(1) some proteins are glycosylated at serine and threonine residues(O-linked glycosylation),
(2) phosphorylation of sugars; (3) addition of sulfate; (4) cleavage of "extra" sequences to convert inactive digestive enzymes or hormones to active digestive enzymes, hormones (why are digestive enzymes, hormones initially produced in an inactive form, and not activated until they reach the Golgi, or secretory vesicles?)

Protein Sorting and Secretion (Ch. 9, p. 362-372)
Proteins transported in vesicles from ER to Golgi, and through Golgi
Proteins have "tags" or "address labels" that direct them to different destinations within the cell
Examples: Proteins with KDEL (lys-arg-glu-leu) sequence return to ER membrane Proteins that will become lysosomal proteins are phosphorylated at their mannose residues--Pathway of lysosomal enzymes from ER to lysosome-
Secretory proteins-examples;
pathway for secretory proteins: ER à Golgi àsecretory vesicles àexocytosis
Transport from Golgi to cell surface--exocytosis
Mechanisms of vesicular transport--(Ch. 9, p. 372-378) How vesicles recognize and fuse with target membranes--role of v-SNARES and t-SNARES, Rab GTPases , GTP, SNAPs, NSF

Import of proteins into mitochondria and chloroplast--(Ch. 10, p.389-395; 405-408)
Mitochondrial and chloroplast genomes--circular DNA, chloroplast genome larger; types of RNAs, proteins coded by mito, chloroplast genomes; types of proteins coded by nuclear genome and imported into the mitochondria or chloroplast
Import--how cytoplasmic proteins are targeted for mitochondria and chloroplast (signal peptides), how these proteins are inserted into mitochondrial (or chloroplast) inner membrane, into intermembrane space, into matrix, or into thylakoid space (chloroplast)

Transport of large particles by endocytosis and phagocytosis--Ch. 12, p. 492-500)
Differences between endocytosis and phagocytosis
Fate of most endocytic vesicles once they are inside the cell (eventually fuse with lysosome and contents broken down)
Pinocytosis--definition, non-specific, small vesicles formed, visualized in capillary endothelial cells
Receptor-mediated endocytosis In eukaryotic cells, most macromolecules are internalized by receptor-mediated endocytosis-for example hormones(insulin, leuteinizing hormone-LH, follicle-stimulating hormone-FSH, growth hormone, prolactin, glucagon), growth factors(epidermal growth factor, platelet-derived growth factor, transforming growth factor b, nerve growth factor), enzymes, serum proteins, antibodies, lymphokines (interleukins, tumor necrosis factor, interferon, colony stimulating factor), nutrients (cholesterol, iron), some viruses and bacterial toxins
Examples of proteins and particles taken up by receptor-mediated endocytosis
Basic structure of coated pits, coated vesicle
Receptor-mediated endocytosis pathway-

Example: cholesterol uptake by receptor-mediated endocytosis: cholesterol is packaged into low-density lipoprotein (LDL) particles. LDL particles consist of a circular monolayer of phospholipid with a protein (apo-B) embedded in the monolayer. Each particle has about 500 free cholesterol molecules in the lipid monolayer and about 1500 cholesterol esters in the interior of the particle. LDL receptors on the surface of most cells recognize and bind the apo-B protein of the LDL particle. Following internalization and movement through the RME pathway, the LDL particles reach the lysosome where the apo-B protein is degraded to amino acids, and the cholesterol esters are hydrolyzed to fatty acids and cholesterol. The cholesterol can then be used by the cell (part of the cell membrane, precursor to steroid hormones). Persons with familial hypercholesterolemia (FH) have too much cholesterol in the blood and die at an early age of heart attacks caused by atheroschlerosis. Found that FH patients lacked the apo-B protein, or had defective LDL receptors.
Formation of plaques in atherosclerosis

Phagocytosis--types of cells where occurs, how occurs--zipper reaction, fusion with membranes (AIDS virus); fate of phagocytic vesicles

Cell-to-Cell Signaling: Hormones, Receptors, and Signal Transduction
Ch. 13, p. 523-553)
Signal Transduction-Flow of information during cell signaling
Second messengers and G-protein-coupled receptors (Ch 13, p. 532-535; 539-542)
Cyclic AMP, a second messenger synthesized through the action of a G protein
Cellular responses mediated by cyclic AMP
How cyclic AMP is synthesized-role of hormone binding to G-protein linked receptor, G protein, adenylyl cyclase
Glucose mobilization in response to epinephrine (adrenaline), an example of a response induced by cAMP.
(1) cAMP activates a protein kinase (PKA-A kinase-cAMP-dependent protein kinase);
(2) cAMP protein kinase begins series of phosphorylations which activate enzymes to breakdown glycogen, inactivate enzyme for glycogen synthesis;
(3) cAMP protein kinase phosphorylates (activates) an inhibitor of phosphoprotein phosphatase (when inhibited this molecule cannot remove phosphate groups from enzymes involved in glycogen breakdown and synthesis);
(4) low levels of cAMP-inhibitor no longer active so process reversed (glucose -->glycogen)

Many steps amplify effect of hormone

Phosphoinositide (inositol phospholipid) pathway to produce second messengers, DAG(activates protein kinase C-PKC) and IP3 (stimulates release of Ca2+ from ER)
(Ch. 13, p. 543-547)
Examples of signals that act through the phosphoinositide pathway; responses generated
Pathway: (1) Signaling molecule binds to its receptor, an integral membrane protein;
(2) Binding of signaling molecule to its receptor activates a G protein;
(3) the G protein activates phospholipase C which breaks down PIP2 into DAG and IP3:
(4) DAG activates protein kinase C (PKC) which phosphorylates substrates eventually leading to a cellular response;
(5) IP3 stimulates release of Ca2+ from the ER (calcium is necessary for the activation of many enzymes)
Example-regulation of growth in epidermal cells; role of protein kinase C

Signaling pathway for stimulation of cell proliferation by growth factors-the receptor tyrosine kinase-Ras (RTK-Ras) signaling pathway, also called the MAP kinase signaling pathway
(Ch. 13, p. 528-530; 534-539; 547-551)
Examples of protein growth factors and their actions
Steps in the RTK-Ras (MAP kinase) signaling pathway-the steps leading to activation of transcription factors which in turn activate genes involved in cell proliferation
(1) Growth factor binds to its receptor, a receptor protein-tyrosine kinase;
(2) The receptor protein-tyrosine kinase phosphorylates itself, which activates adaptor proteins;
(3) Adaptor proteins activate Ras, a membrane associated G protein;
(4) Ras activates Raf which phosphorylates and activates MEK which phosphorylates and activates MAP kinase (mitogen-activated protein kinase);
(5) MAP kinase phosphorylates and activates transcription factors which activate genes involved in cell proliferation

PKC and PKA can activate intermediates in the RTK-Ras (MAP kinase) signaling pathway, and PKA can also directly activate transcription factors

Cell Cycle Regulation (Ch 14, p. 571-577; 579-582; 590-592)
Stages of cell cycle
Checkpoints-control points in the cell cycle
Control of cell cycle-Cdk (cyclin-dependent kinase; also called cdc2 kinase) combines with G1 cyclins synthesized during G1 to trigger S phase; G1 cyclin degraded during S phase to trigger entry into G2; mitotic cyclin combines with Cdk to form MPF (mitosis promoting factor) which triggers mitosis; G2 cyclin is degraded during mitosis to start G1 again.

Role of tumor suppressor gene products and oncogene products in control of cell proliferation

Cell Motility and Shape--The Cytoskeleton and Cellular Movements
4 types of fibers which make up the cytoskeleton
Cytoskeletal interconnections

Microtubules (Ch. 11, p. 446-463)
Structure of microtubules (Ch. 11, p. 446-447)
Assembly of microtubules (Ch 11, p. 446-452)
Role of MAPs-function in establishing dendrites and axons, role in Alzheimer's disease
MT assembly associated with microtubule organizing centers (MTOC)--basal bodies (cilia, flagella), centrosome (amorphous region near nucleus which contains centrioles in animal cells)

Movement of vesicles, organelles along MT (Ch. 11, p. 452-457)
role of kinesin and dynein in transport of particles along MT

Movement of cilia and flagella (Ch 11, p. 458-461)
Structure of cilia, flagella
How cilia move-how MT interact to cause bending (beating) of cilia, including the dynein crossbridging

Role of microtubules in movement of chromosomes during mitosis
(Ch. 11, p. 449-450; 457-458; Ch 14, p. 587-590)
Structure of mitotic spindle-MT; MTOC (centrosome); MAPs; movement of centrioles during cell cycle
Kinetochore structure, location (Ch. 4, p. 150-154)
Fibers-kinetochore, polar, astral
Movements of MT spindle fibers during prophase
How chromosomes align at the equator during metaphase. Why do chromosomes align at equator of cell during metaphase of mitosis?

Distinguish between anaphase A and anaphase B
How spindle MT could move the chromosomes to the poles during anaphase, using a "depolymerization/kinetochore movement" model to account for chromosome-to-pole movement (Anaphase A) and a "polymerization/sliding MT" model to account for elongation of polar MT (Anaphase B)

Role of MT in cytokinesis in plants; formation of cell plate (Ch 14, p. 593-594)

Microfilaments and Intermediate filaments
Role of cytoskeleton in muscle contraction (Ch 11, p. 421-425; 432-439)
Structure of actin microfilaments, myosin
Structure of skeletal muscle--myofibrils, thick filaments, thin filaments, sarcomere, Z line; muscle proteins stabalize interaction between filaments, and connection to membrane
How myosin moves along actin filaments using ATP hydrolysis to cause muscle contraction
Myosin-linked regulation of muscle contraction--Ca2+ binds calmodulin; complex activates kinase enzyme which phosphorylates light chains of myosin
Actin-linked regulation of muscle contraction--triggering of muscle contraction by nerve impulse--impulse spreads through transverse tubules to sarcoplasmic reticulum which releases Ca 2+; calcium binding to troponin-C changes position of tropomyosin so the myosin heads can bind actin filaments

Actin filaments in non-muscle cells( Ch. 11, p. 425-432; 439-440)
Explain how lamellipodia of cells such as fibroblasts (or filapodia of nerve growth cones) extend to cause movement
Explain amoeboid movement of cells such as amoebas and macrophages
Examples of actin (or actin-myosin) functioning in non-muscle cells
Function of actin filament bundles in microvilli
Function of actin-myosin (and microtubules) in contractile ring of furrow (Ch. 14, p. 593-594)
Role of actin and MT in changes of cell shape during development
Function of actin stress fibers
Function of actin filaments in the acrosome
Actin-binding proteins--how they interact with actin, functions
Role of signal transduction systems (pathways) in motility and organization of cytoskeleton

Intermediate filaments (Ch. 11, p. 440-446)
Function of intermediate filaments found in various cells types
Structure of intermediate filaments
Types of intermediate filaments--where found

Cell-Cell Adhesion and Communication
Cell junctions--description, function(s)
Desmosomes, hemidesmosomes (Ch. 11, p.443-445)
Adherens junctions (adhesion belts) (Ch. 11, p. 430-431)
Tight junctions (Ch. 12, p. 513-514)
Gap junctions (Ch. 12, p. 514-515)
The Extracellular Matrix (Ch. 12, p. 504-510)
Structure of collagen
Proteoglycans, glycosaminoglycans-structure, properties, functions, properties of proteoglycans which contribute to their ability to resist compression
Proportion of collagen to proteoglycans in different types of connective tissue
Elastin-structure, functions
Fibronectin-structure, functions
Laminin-structure, functions
Basal lamina-structure, where found, functions

Cell-Cell Adhesion and Communication
Cell Adhesion molecules (CAMs) (Ch. 12, p. 510-513)
Integrins-structure, role in cell-matrix interactions
Other cell adhesion molecules participate in cell-cell adhesion-cadherins,
Ig-superfamily CAMs (eg., N-CAM), selectins, mucin-like CAMs
Mechanisms by which CAMs mediate cell-cell adhesion
Role of cadherins in development of embryo
Role of CAMs in leukocyte extravasation during inflammation and metastasis

Summary of junctional and non-junctional adhesive mechanisms

Transport across Cell Membranes (Ch. 2, p. 81-84; Ch 12, p. 476-491)
Types of molecules permeable, impermeable to lipid bilayer
Diffusion-how molecules cross membrane, how water crosses membrane,
high -> low concentration, exergonic, factors which affect rate of diffusion
Facilitated diffusion-specific transport proteins required--why needed, high to low concentration, saturable
Explain how a molecule such as glucose enters membrane by carrier mediated facilitated diffusion
Ion channels
types of ions transported, structure of ion channel transport proteins, types of "triggers" to open/close channels, examples;
how ion channels operate in transmission of nerve impulse
Active transport
movement against concentration gradient, energy provided by ATP or concentration gradient of certain ions
Explain how the Na+ - K+ pump(Na+ - K+ ATPase) works
Co-transport-indirect active transport-symport, antiport
Explain transport of glucose across epithelial cells(eg., intestinal epithelium) by glucose - Na+ symport, how the Na+-glucose symport protein works
H+-lactose symport in bacteria
Antiports-H+-Ca2+, H+-Na+, H+-sucrose-in plant vacuole membrane-how they work, function