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Literature summary for 5.6.1.1 extracted from
- A common substrate recognition mode conserved between katanin p60 and VPS4 governs microtubule severing and membrane skeleton reorganization (2010), J. Biol. Chem., 285, 16822-16829.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| a glutathione S-transferase-tagged form of kp60-NTD expressed in Escherichia coli BL21 (DE3) | Mus musculus |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| the structure of kp60-NTD reveals a striking similarity to those of the microtubule interacting and trafficking domains (MIT). The arragnement of helices 2 and 3 is well conserved between kp60-NTD and the MIT domain from Vps4, a homologous protein that promotes disassembly of the endosomal sorting complexes required for transport III membrane skeleton complex. The positively charged surface formed by helices 2 and 3 binds tubulin | Mus musculus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mus musculus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant glutathione S-transferase-tagged form kp60-NTD, affinity purification on glutathione-Sepharose and dialysis | Mus musculus |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | a single domain isolated from the N-terminus of mouse katanin P60 binds to tubulin | Mus musculus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| katanin p60 | - |
Mus musculus |
| kp60-NTD | - |
Mus musculus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | katanin p60, a microtubule-severing enzyme plays a key role in cytoskeletal reorganization during various cellular events in an ATP-dependent manner | Mus musculus |
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Release 2023.1 (January 2023)
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