Correction: Hsueh et al., "Bipartite Interaction between Neurofibromatosis Type I Protein (Neurofibromin) and Syndecan Transmembrane Heparan Sulfate Proteoglycans".

نویسندگان

  • Yi-Ping Hsueh
  • Anne M. Roberts
  • Manuela Volta
  • Morgan Sheng
  • Roland G. Roberts
چکیده

In the article “Bipartite Interaction between Neurofibromatosis Type I Protein (Neurofibromin) and Syndecan Transmembrane Heparan Sulfate Proteoglycans” by Yi-Ping Hsueh, Anne M. Roberts, Manuela Volta, Morgan Sheng, and Roland G. Roberts, which appeared on pages 3764 –3770 of the June 1, 2001 issue, “In B, the same protein samples were used to analyze the subcellular fractionation of neurofibromin, syndecan-3, CASK, and PSD-95. The CASK and syndecan-3 immunoblots have been previously published (Hsueh and Sheng, 1999)” is added to the end of legend of Figure 3 to clarify that the panels of CASK and Synd-3 immunoblots shown in Figure 3B had been previously published as panels CASK and Syn-3C-2 in Figure 3A of the article “Regulated Expression and Subcellular Localization of Syndecan Heparan Sulfate Proteoglycans and the Syndecan-Binding Protein CASK/LIN-2 during Rat Brain Development” by Yi-Ping Hsueh and Morgan Sheng, which appeared on pages 7415–7425 of the September 1, 1999 issue. The panels “Synd-3” and “Syn-3C-2” in these two papers are identical data showing the subcellular fractionation of syndecan-3 in brain tissue. The different labeling of the identical immunoblots is because two different syndecan-3 antibodies named Syn-3ecto and Syn-3C-2 (which recognize extracellular and C-terminal domains in syndecan-3, respectively) were used in the Hsueh and Sheng 1999 study. In the 2001 paper, only the Syn-3C-2 antibody was used for immunoblotting of syndecan-3. To simplify the figure labeling in Figure 3B of the Hsueh et al. 2001 paper, we labeled it as Synd-3 instead of Syn-3C-2. This correction does not affect the conclusions of the paper.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Bipartite interaction between neurofibromatosis type I protein (neurofibromin) and syndecan transmembrane heparan sulfate proteoglycans.

The neurofibromatosis type 1 (NF1) gene encodes a large tumor suppressor protein (neurofibromin). Although it is known to possess Ras GTPase-activating protein (GAP) activity, the cellular role of neurofibromin remains unclear. Here we used yeast two-hybrid screening to identify neurofibromin-interacting proteins. Syndecan-2, a transmembrane heparan sulfate proteoglycan (HSPG), was isolated as ...

متن کامل

Syndecan-Regulated Receptor Signaling

The syndecans are transmembrane heparan sulfate (HS) proteoglycans expressed on all adherent cells (Bernfield et al., 1999; Rapraeger and Ott, 1998). A family of four, they have diverse functions ranging from participation in cell–cell adhesion, regulation of the signaling of HS binding growth factors, and organization of cell–matrix adhesion and signaling. A paper published in this issue of Th...

متن کامل

Specific structural features of syndecans and heparan sulfate chains are needed for cell signaling.

The syndecans, heparan sulfate proteoglycans, are abundant molecules associated with the cell surface and extracellular matrix and consist of a protein core to which heparan sulfate chains are covalently attached. Each of the syndecan core proteins has a short cytoplasmic domain that binds cytosolic regulatory factors. The syndecans also contain highly conserved transmembrane domains and extrac...

متن کامل

Heparan Sulfate Proteoglycans in Infection

To cause infections, microbial pathogens elaborate a multitude of factors that interact with host components. Using these host–pathogen interactions to their advantage, pathogens attach, invade, disseminate, and evade host defense mechanisms to promote their survival in the hostile host environment. Many viruses, bacteria, and parasites express adhesins that bind to cell surface heparan sulfate...

متن کامل

Syndecan-1: an inhibitor of arterial smooth muscle cell growth and intimal hyperplasia.

OBJECTIVE Arterial injury induces smooth muscle cell (SMC) proliferation, migration, and intimal accumulation of cells and extracellular matrix. These processes are regulated by the administration of the glycosaminoglycans heparin and heparan sulfate, but little is known about the role of endogenous heparan sulfate proteoglycans in the vessel wall. We investigated the response to carotid injury...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Journal of neuroscience : the official journal of the Society for Neuroscience

دوره 37 5  شماره 

صفحات  -

تاریخ انتشار 2017