Talk:Epsin

=Comments From Cdxaam=

Untitled
Overall, the information is great. The statements not seem to violate and plagiarism from the cited sources and the sources so far add greatly to the article. Below are some suggestions that should improve the quality of the article:

- Will work on grammar and read closely for style errors
 * Sentence structure and style could be tweaked for clarity in all the sections once formatting is completed.

- Fixed it! Good point.
 * The citations for the sources in the first section should follow the sentences individually rather than lumping them all at the end. In line citations follow Wikipedia's Suggested style guidelines.

- Was trimmed down by another Wiki user.
 * The introduction seems lengthy. If possible, trim down the introduction and allocate the information into other subsections.

- Fixed by other Wiki user
 * Similarly, the "Structure" section could use some formatting since every citation is the same source.

- Fixed by other Wiki User
 * The phrase "It has also been postulated that..." is potentially unnecessary. Rephrase the information or cite a source so as not to violate articles rules about what is factual and what is not entirely supported.

- Thanks for the comments. They were all super helpful. I will work on adding them for our class project. Lnbond92 (talk) 17:22, 28 April 2015 (UTC)
 * Additional links to other wikipedia articles could be added to integrate the article further. Attempt to link each epsin protein to their own individual article (like epsin-1) should they exist. Schizophrenia, E. Coli, homologue (sp?), and other important topics necessary for the information to be relevant that may not be understood by the user should probably be hyperlinked, without overlinking.

Cdxaam (talk) 23:26, 9 April 2015 (UTC)

Comments from Cdeclue7
The article is coming along, but could use more additions to push it into a Good Article category. - Added a picture of clathrin coated vesicles and a crystal structure of the ENTH domain since all Epsins contain an ENTH domain — Preceding unsigned comment added by Lnbond92 (talk • contribs) 20:16, 11 May 2015 (UTC) - Got a bit into this in a review article I used. I am trying to stick to review articles for the majority of my contributions but I will add to the future reading section. - Couldn't get to more than the abstract but added what I could. Thanks for the link!! - I have actually already read through and took a lot of information from this paper. It is super helpful for this page. Cdeclue7 (talk) 15:38, 28 April 2015 (UTC)
 * Consider adding pictures, such as membrane blebbing and clathrin-coated vesicles.
 * Consider adding its role in breast cancer in the clinical implications section (Cai, Xiaofeng, et al. 2013. Upregulation of epsin in breast cancer and critical role of epsin in promoting cancer growth and metastasis. Cancer Research 73(8): 5128-5128)(Cai, Xiaofeng, and Hong Chen. 2014. Epsin promotes breast cancer progression and metastasis by controlling nf-κb activation. Cancer Research 74(19): 3292-3292).
 * There has recently been found to be a link between epsin and wnt signaling in colon cancer (Chang, Baojun, et al. 2015. Epsin is required for Dishevelled stability and Wnt signalling activation in colon cancer development. Nature communications 6).
 * I would also add what is known about epsin's influence on cell signaling, such as notch signaling and RhoGTPases (Sen, Arpita, et al. 2012. The epsin protein family: coordinators of endocytosis and signaling. Biomolecular concepts 3(2): 117-126).

= Removed section =

The following section may be correct, but the content looks unreadable even for the most of biologists. I actually do not know how to simplify it properly. Maybe it would be better to get without it:

Epsin1
Epsin 1 is a brain enriched 94 kDa protein that interacts with ubiquitin via its UIM domains, it interacts with the EH domains of Eps15 and Eps15R via its 3 NPF motifs, it interacts with the alpha appendage domains of AP2 adaptors via DPW motifs and it interacts with clathrin via its clathrin terminal domain binding motifs. This same domain has motifs for clathrin interactions. Given the PtdIns(4,5)P2 specificity of epsin1 and epsin2 they are assumed to be plasma membrane adaptors.

Epsin3
Epsin 3 is almost exclusively localised to migrating keratinocytes in cutaneous wounds.

EpsinR
Epsin 4/EpsinR/enthoprotin/Clint is thought to be involved in the budding of clathrin-coated vesicles from intracellular compartments. It binds to AP1 adaptors rather than AP2.

pubmed
 * Kay BK, Yamabhai M, Wendland B, Emr SD. (1999) Identification of a novel domain shared by putative components of the endocytic and cytoskeletal machinery. Protein Sci. 8, 435-8. pubmed
 * Itoh T, Koshiba S, Kigawa T, Kikuchi A, Yokoyama S, Takenawa T. (2001) Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis. Science. 291, 1047-51. pubmed
 * Ford MG, Mills IG, Peter BJ, Vallis Y, Praefcke GJ, Evans PR, McMahon HT. (2002) Curvature of clathrin-coated pits driven by epsin. Nature 419, 361-6. pubmed
 * Stahelin RV, Long F, Peter BJ, Murray D, De Camilli P, McMahon HT, Cho W.(2003) Contrasting membrane interaction mechanisms of AP180 N-terminal homology (ANTH) and epsin N-terminal homology (ENTH) domains. J. Biol. Chem. Aug 278, 28993-9. pubmed

Audriusa 17:17, 8 April 2007 (UTC)

Developmental Biology Project
Hello, I am talking on this page as part of this assignment and here's a link to my sandbox. This page could use more on Epsin's implication in clathrin coated vesicle formation and how that affects signaling events such as developmental and defense in both mammalian and plants. — Preceding undated comment added 16:35, 11 February 2015 (UTC) 16:51, 26 February 2015 (UTC) Lnbond92 (talk) 16:52, 26 February 2015 (UTC)