Foundations in Biology

EXAM #2
SELF-LECTURE REVIEW:
COLLECTION OF KEY TERMS
SECTION 1

Cell Communication (Cell Signaling)

Signal reception
Signal transduction
Signal amplification
Cellular response
Signal termination
Contact-dependent signaling
Heparin sulfate proteoglycans immobilize signaling proteins
Cell-surface receptors
Small, hydrophilic ligand
Trans-membrane protein
Cytoplasmic receptors
Hydrophobic ligand
Steroids
Nonpolar (hydrophobic) R-groups of the receptor would interact with the nonpolar ligand.
Directed transport to the nucleus and alter gene expression.
Nuclear pore has guarding proteins for selective entry.
Shape change of receptor-signal complex allows for nuclear localization signal sequence (NLS) to be exposed on
protein surface (lysines and arginines)
G-protein coupled receptors (GPCR)
Trimeric GTP-binding protein (G-protein) normally bound to GDP, replace it with GTP when stimulated by the
conformational change of GPCRs after their R-groups interact with the ligand
GTPase-activating proteins drive protein into off state by increasing rate of hydrolysis of bound GTP
Adenylyl cyclase: ATP to cAMP
Second messengers are water soluble and diffuse in the cytosol. Others (e.g. diacylglycerol) are lipid-soluble and
can pass through plasma membrane.
Protein kinases (vs. phosphatases: remove phosphate groups from proteins) activate effector proteins
Phosphodiesterases degrade cAMP to AMP which stops the phosphorylation and activation of target proteins by
PKA.
Receptor tyrosine kinases (RTK)
RTKs phosphorylate each other and activate intracellular signaling pathways.
Bind signaling molecules, dimerize, phosphorylate each other, and activate.
Each member of the receptor pair attaches a phosphate group to the other member.
The attached phosphate groups provide binding sites for intracellular signaling proteins.
Cytoplasmic signaling proteins
Ras is bound to GDP and inactive. Once activated, releases GDP and binds to GTP.
Involved in MAP kinase pathway (Mitogen-activated protein kinase)
G-protein, like Ras, is a GTPase. can deactivate itself by converting GTP to GDP, once contact-dependent
signaling is lost (the ligand is unbound to the receptor).

SECTION 2

Cell Form and Function

Tubulin dimers
Microtubules
Kinesin & dynein
Actin monomers
Microfilaments
Myosin move cargo along microfilaments.
Microfilaments add actin proteins and remove actin proteins to grow and shrink the length of the microfilament. Net
growth at one end and removal at the other leads to movement of the microfilament.
ATP is used to change the shape of the myosin motor protein: energy and the phosphate groups change R-group
interactions. It is used in the polymerization and depolymerization cycles of actin addition/removal for
microfilament dynamics.
Intermediate filaments
Composed of lamins: nucleus
Composed of keratins: cytoplasm
ATP/GTPi (hydrolysis)
Diffusion
Cytoskeleton-mediated transport (vesicles in the secretory pathway)
Cell crawling
Pseudopods
Muscles/microfilaments
Cell swimming
Cilia and flagella
Microtubules
9+2 arrangement of microtubules
Microtubule doublets
Dynein arms
ATP hydrolysis for dynein arm movement between microtubule doublets
Myosin motor protein motion <microfilament dynamics> via ATP hydrolysis
Role of Ca2+ : myosin binding sites covered by tropomyosin. Troponin binds calcium ions and exposes
myosin binding sites