more obscure proteins and agents we need to know.

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32 Terms

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Filamin

Cross links microfilaments into a gel like network. (Fillament-crosslinking protein)

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Villin

Villin bundles actin in microvilli. (Filament-bundling protein)

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Fimbrin

Bundles actin filaments in parallel arrays. (Filament-bundling protein)

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Alpha actinin

Links actin filaments into parallel arrays at the z-line in sarcomeres. (Filament bundling protein)

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Spectrin

Forms a network under plasma membrane providing support. Helps other proteins bind to membrane (E.g dynactin complex will bind to membrane associated spectrin during power stroke step of calcium cycle).

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Takin

Links actin filaments to integrins at focal adhesions. Binds to vinculin and alpha actinin which can bind directly to actin MFs.

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Dystrophin

Large protein found at muscle costameres that is part of a complex of proteins that attaches the muscle cell plasma membrane to the extracellular matrix. “Links actin cytoskeleton to ECM in muscle cells”

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Thymosin B 4

Sequesters actin monomers, preventing polymerization in MFs. (Monomer-sequestering protein)

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Profilin

Appears to compete with Thyomisin beta 4 for binding to G-actin monomers. “Facilitates actin polymerization by promoting ATP change.” (Monomer-polymerizing proteins)

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Cofilin

“Cofilin severs filaments, creating new plus and minus ends.” “Severs actin filaments and promotes turnover”

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Gelsolin

“Functions by breaking actin MFs and capping their newly exposed plus ends, thereby preventing further polymerization.” (Labeled as Filament-Severing protein though)

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Formin

Nucleate linear actin filament growth (Actin-polymerizing proteins).

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Capz

Caps MF at barbed end (plus end) to regulate growth of MFs. (Filament-capping proteins)

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Cortactin

Stabilizes branched actin networks. Not even in the book idk man…

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Tropomodulin

Caps pointed ends (minus end) of F-actin.

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Arp2/3 complex

Complex of actin-related proteins that allow the actin monomers to polymerize as new “branches” on the sides of existing MFs. Facilitates nucleation of MFs.

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Types of actin binding proteins (and some examples)

Monomer sequestering proteins (thymosin beta 4), Actin-polymerizing proteins (formin), Filament- severing proteins (gelsolin), Filament -capping proteins (capz), filament-crosslinking proteins (filamin), filament-bundling proteins (alpha actinin and fimbrin)

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Colchicine/ colcemid

Binds to beta tubulin, inhibits assembly

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Nocadazole

Binds beta tubulin, inhibits polymerization.

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Vinblastine/ vincristine

Aggregates tubulin heterodimers

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Paclitaxel (Taxol)

Stabilizes microtubules

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Agents affecting microtubules (that he told us to memorize)

Colchicine/ colcemid, Nocadazole, Vinblastine/ vincristine, paclitaxel (Taxol).

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Agents affecting Microfilaments (that we need to know)

Cytochalasin D, Latrunculin A, Phalloidin.

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Agents affecting IFs (hint only one)

Acrylamide, causes loss of intermediate filament networks.

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Cytochalasin D

Prevents addition of new monomers to plus ends of Mfs

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Latrunculin A

Sequesters actin monomers in Mfs

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Phalloidin

Binds and stabilizes assembled Mfs

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Rac

Member of a family of Rho GTPases (monomeric G proteins that are localized to the plasma membrane where a lipid modification keeps them attached to the inner leaflet of the plasma membrane). Rac stimulates formation of various actin-containing structures within cells. Active when bound to GTP

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Cdc42

Part of the Rho GTPases (monomeric G proteins that are localized to plasma membrane through a lipid modification that keeps them attached to the inner leaflet of the plasma membrane). Stimulates formation of various actin-containing structures. Active when bound to GTP

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Rho GTPases

Family of monomeric G proteins, which include Rho Rac and Cdc42, that stimulate formation of various actin-containing structures within cells. They give rise to the dramatic change seen in the cytoskeleton when exposed to growth factors.

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Inositol phospholipids

Inositol phospholipids are a type of membrane phospholipid that regulates actin assembly. One species PIP2 can bind to profilin, Capz and recruit them to the plasma membrane.