L4: Microtubule motor proteins and IMFs Flashcards
What directionality do the two types of motor protein have?
Kinesins are anteretrograde, dyneins are retrograde
Main domains of kinesin with function
Head domain (motor that generates movement), neck (flexible, determines direction)
Kinesin 1 vs 5
Kinesin 5 is bipolar (2 globular bulbous regions where antibodies bind)
Cytosolic dyneins
Retrograde, have an ATPase domain and a MT binding domain. Linked to their cargos (vesicles/chromosomes) by dynactin complexes.
How would a cargo change direction?
Able to interact with a different type of motor proteinh
How fast do kinesins travel?
600nm/s
Structure of cilia and flagella
Axoneme (core), with 9 outer doublet MTs and 2 central pair. Outer doublet MTs have 13-protofilament and 10-protofilament
How do C + F move?
Axonemal dyneins generate force by sliding outer doublet MTs past each other causing bending due to constraints by nexin crosslinks
Directionality of MTs in mitosis?
(-) end associates with spindle poles for all types
Kinetochore MTs
Connect chromosomes by kinetochore attachment site to spindle pole
Polar MTs
Hold and control distance between poles
Astral MTs
Radiate towards cortex of cell; help position spindle and determine plane of cytokinesis
Compare IMF with MTs
IMFs are less dynamic, unpolarized, have no motors, more stable. Therefore used for cell and tissue strength and integrity
Class 1 IMFs (protein, distribution, function)
Made of acidic keratins, found in epithelial cells, provide tissue strength and integrity
Class 2 IMFs (protein, distribution, function)
Made of basic keratins, found in epithelial cells, provide tissue strength and integrity
Class 3 IMFs (protein, distribution, function)
Made of desmin, GFAP, vimentin, found in muscle/glial/mesenchymal cells, provide sarcomere organization
Class 4 IMFs (protein, distribution, function)
Made of neurofilaments, found in neurons, provide axon organization
Class 5 IFs (protein, distribution, function)
Made of lamins, found in nuclei, provide nuclear structure and organization
Why are IMFs stable?
Due to alpha-helical rod structure, overlap along long axis to provide a rope-like filament
Basic IMF structure
10nm diameter, globular N- and C-terminal domains joined by central alpha-helical core/rod domain
IFAPs (with example)
Intermediate filament associated proteins which connect IFs together and to MTs, eg Plakin
Application of IMFs
Tissue specific so make good markers for cell types (eg Stem Cells)
Epidermolysis Bullosa
Caused by mutation in Keratin 14 gene