User:Emw17b/sandbox

Outline
1) summarize your article and says why it is important that it be accurate and updated

The “microtubeule nucleation” articles provides a brief overview of the dynamic process of microtubule nucleation and can be expanded. This is an important article to update because microtubules play a vital role in regulation of many cellular processes, including mitosis and meiosis. The complex temporal and spatial regulation of MT nucleation proves a powerful mechanism to control such cellular processes. Also, MT nucleation is mentioned on the the “microtubule” main page in a subheading entitled “nucleation”. There is a large amount of overlap between these two pages and the main page of MT nucleation could include more details about the many recent advancements by scientist that have uncovered multiple MT nucleation pathways.

2) name specifically which parts, sections, or paragraphs assigned to you.

I will edit Section 1: "Role of γ-tubulin and the γ-tubulin ring complex (γ-TuRC)" on the MT nucleation main page

3) summarize your plan or suggestions for improvement (i.e. discuss what to improve, not yet making the specific edits - just your plan for the instructor to review and give feedback.

I plan to include more citations to support the text that is already present in this section. Also, I plan to include information about the gamma-Tubulin Small Complex (gamma-TuSC), the proteins that comprise this complex (GCP2, GCP3 and two gamma-tubulin molecules), and their homologs in different species. Also, I think it is important to specify that the gamma-TuRC includes gamma-TuSCs in addition to GCP4, GCP5, and GCP6. With such changes, it may be a good idea to change the title of the heading to either include gamma-TuSC or to be more broad term of " γ-TuCs" rather than TuRC. Lastly, I hope to include a picture or figure of these complexes.

4) Create a section in your Sandbox titled "Bibliography" and compile a list of relevant, reliable books, journal articles, or other sources that you will use to support your work. Post that bibliography to the talk page of the article you'll be working on, and in your sandbox. Make sure to check in on the Talk page to see if anyone has advice on your bibliography.

Original Text:
In vivo, cells get around this kinetic barrier by using various proteins to aid microtubule nucleation. The primary pathway by which microtubule nucleation is assisted requires the action of a third type of tubulin, γ-tubulin, which is distinct from the α and β subunits that compose the microtubules themselves. The γ-tubulin combines with several other associated proteins to form a conical structure known as the γ-tubulin ring complex (γ-TuRC). This complex, with its 13-fold symmetry, acts as a scaffold or template for α/β tubulin dimers during the nucleation process—speeding up the assembly of the ring of 13 protofilaments that make up the growing microtubule. The γ-TuRC also acts as a cap of the (−) end while the microtubule continues growth from its (+) end. This cap provides both stability and protection to the microtubule (-) end from enzymes that could lead to its depolymerization, while also inhibiting (-) end growth.

Revisions for "Role of gamma-tubulin and the gamma-tubulin ring complex (gamma-TuRC)" in "Microtubule nucleation" main page:
"Role of γ-tubulin and γ-tubulin complexes (γ-TuCs)" (Suggested new title for this section)

In vivo, cells get around this kinetic barrier by using various proteins to aid microtubule nucleation. The primary pathway by which microtubule nucleation is assisted requires the action of a third type of tubulin, γ-tubulin, which is distinct from the α and β subunits that compose the microtubules themselves. The γ-tubulin combines with several other associated proteins to form conical structures known as γ-tubulin complexes (γ-TuCs). The γ-TuCs have 13-fold symmetry and act as a scaffold or template for α/β tubulin dimers during the nucleation process—speeding up the assembly of the ring of 13 protofilaments that make up the growing microtubule. The localization of γ-TuCs to MTOC s regulate temporal and spatial MT nucleation. One such γ-TuC, known as the γ-tubulin small complex (γ-TuSC) is comprised of two γ-tubulin molecules that bind to Spc97/GCP2 and Spc98/GCP3. These γ-TuSCs are sufficient for MT nucleation and have been shown to self-oligomerize under the control of cell-cycle dependent Spc110-N phosphorylation in S. cerevisiae. In higher eukaryotic model systems, γ-TuSCs oligomerize and can template the formation the γ-tubulin ring complex (γ-TuRC) by the binding of additional proteins containing the conserved Spc97_Spc98 domain, known as GCP4, GCP5, GCP6. In addition, the γ-TuRC also acts as a cap of the (−) end while the microtubule continues growth from its (+) end to provide both stability and protection to the microtubule (-) end from enzymes that could lead to its depolymerization, while also inhibiting (-) end growth. γ-TuSC and γ-TuRCs may have distinct MT nucleation regulatory roles as GCP4, 5, and 6 are absent from interphase MTOCs and restricted to spindle pole bodies in S. pombe . γ-TuC proteins are highly conserved throughout many organisms suggesting an evolutionary conserved mechanism for MT nucleation.