User:Alisa Cario

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[[Image:Stathmin_figure_cario1.png|center|thumb| upright=3| Figure 1. Adapted from ''Ruben 2004''. Stathmin, in purple, can bind to tubulin dimers to prevent polymerization or to microtubules to increase the rate of catastrophe. ]]
[[Image:Stathmin_figure_cario1.png|center|thumb| upright=3| Figure 1. Adapted from ''Ruben 2004''. Stathmin, in purple, can bind to tubulin dimers to prevent polymerization or to microtubules to increase the rate of catastrophe. ]]
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== '''Evolutionary conservation''' ==
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Stathmin belongs to a gene family that have a characteristic stathmin-like domain spanning across eukaryotes. This family includes Stathmin-1, SCG10/stathmin-2, SCILP/stathmin-3, and RB3/stathmin-4. RB3 is alternatively spliced to form RB3, RB3', and RB3" <ref>PMID: 9342231</ref>. SCG10 and SCLIP, are exclusively neuronal proteins, while RB3 is expressed mostly in the brain but some in the adrenal glands <ref>PMID: 8344928</ref> <ref>PMID: 2776625</ref>. Unlike the neuronal proteins, stathmin-1 is ubiquitously expressed in all cell types.
== '''Function''' ==
== '''Function''' ==
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'''Differentiation''': Stathmin family proteins expression are regulated during stages of development. It is regulated in early and late embryogenesis <ref>PMID: 1893566</ref>. Stathmin is regulated in differentiating muscle cells, T lymphocytes, and oligodendryocytes <ref>PMID: 22529300</ref> <ref>PMID: 14603467</ref>. Other family members are regulated in stages in development.
'''Differentiation''': Stathmin family proteins expression are regulated during stages of development. It is regulated in early and late embryogenesis <ref>PMID: 1893566</ref>. Stathmin is regulated in differentiating muscle cells, T lymphocytes, and oligodendryocytes <ref>PMID: 22529300</ref> <ref>PMID: 14603467</ref>. Other family members are regulated in stages in development.
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== '''Evolutionary conservation''' ==
 
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Stathmin belongs to a gene family that have a characteristic stathmin-like domain spanning across eukaryotes. This family includes Stathmin-1, SCG10/stathmin-2, SCILP/stathmin-3, and RB3/stathmin-4. RB3 is alternatively spliced to form RB3, RB3', and RB3" <ref>PMID: 9342231</ref>. SCG10 and SCLIP, are exclusively neuronal proteins, while RB3 is expressed mostly in the brain but some in the adrenal glands <ref>PMID: 8344928</ref> <ref>PMID: 2776625</ref>. Unlike the neuronal proteins, stathmin-1 is ubiquitously expressed in all cell types. All members of this family contain the C-terminal coiled coil domain. However, the binding affinity to tubulin of the protein family members differ <ref>PMID: 11278715</ref>. Interestingly, the neuronal isoforms are known to contain an additional N-terminal domain to affect their localization <ref>PMID: 9788875</ref>.
 
== '''Structure''' ==
== '''Structure''' ==
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====How does the structure relate to it's function?====
====How does the structure relate to it's function?====
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The <scene name='77/778894/Stathmin_nterm/1'>N-terminal region</scene> is known to increase tubulin catastrophe. This region helps destabilize the ends of the microtubule filaments by curving the tubulin dimers at the end, and disrupting lateral hydrogen bonds. The N-terminal region is known as the regulatory domain of the protein, because it is subject to most of the post-translational modifications. This region binds and caps alpha tubulin to accomplish this task <ref>PMID: 9880330</ref>.
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The <scene name='77/778894/Stathmin_nterm/1'>N-terminal region</scene> is known to increase tubulin catastrophe. This region helps destabilize the ends of the microtubule filaments by curving the tubulin dimers at the end, and disrupting lateral hydrogen bonds. The N-terminal region is known as the regulatory domain of the protein, because it is subject to most of the post-translational modifications. This region binds and caps alpha tubulin to accomplish this task <ref>PMID: 9880330</ref>. The neuronal family members are known to contain an additional N-terminal domain to affect their localization <ref>PMID: 9788875</ref>
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The<scene name='77/778894/Stathmin_c_term/1'> C-terminal region</scene>, also known as the interaction domain, is known to sequester tubulin heterodimers. This region is comprised of a <scene name='77/778894/Stathmin_coiled_coil/1'>coiled-coil alpha helix</scene>. This region of stathmin is <scene name='77/778894/Zoom_of_stathmin_on_alpha/1'>known to bind to helix 10 of alpha tubulin</scene>. Helix 10 of alpha tubulin is thought to be important for incorporation into microtubules <ref>PMID: 9880330</ref>.
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The<scene name='77/778894/Stathmin_c_term/1'> C-terminal region</scene>, also known as the interaction domain, is known to sequester tubulin heterodimers. This region is comprised of a <scene name='77/778894/Stathmin_coiled_coil/1'>coiled-coil alpha helix</scene>. This region of stathmin is <scene name='77/778894/Zoom_of_stathmin_on_alpha/1'>known to bind to helix 10 of alpha tubulin</scene>. Helix 10 of alpha tubulin is thought to be important for incorporation into microtubules <ref>PMID: 9880330</ref>. All members of this family contain the C-terminal coiled coil domain. However, the binding affinity to tubulin of the protein family members differ <ref>PMID: 11278715</ref>
== '''Disease relevance''' ==
== '''Disease relevance''' ==

Revision as of 12:54, 30 April 2018

* Full Real Name: Alisa Cario

  • Position: Graduate Student
  • Institution (NO ABBREVIATIONS): University of Vermont
  • City, State/Province, Country: Burlington, VT USA
  • Field of Expertise or Study: Creation of protopedia page for a class project. The class is Proteins 1 under Dr. Stephen Everse


Stathmin-4 (RB3) bound to Tubulin stabilized with Vinblastine 

4eb6

Structure of stathmin bound to two tubulin heterodimers at 3.47Å resolution. Tubulin dimers are stabilized by vinblastin, shown by grey spheres between heterodimers. (PDB entry 4eb6)

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

Alisa Cario, Eric Martz

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