Good news is here for folks on Sprint who've been anxiously waiting for a first taste of LTE connectivity and Ice Cream Sandwich. Google's official Galaxy Nexus website has quietly gone live with a registration section for anyone on the Now Network who wants to be notified when the device goes up for sale. If you'll recall, the pre-release version of Sprint's GNex that we spent time with at CES notably retained access to Google Wallet, and was apparently free of any crapware (unlike Verizon's variant). Aside from that -- and a Sprint logo -- it's essentially the same 32GB device you've come to know in the US. There's still no word on pricing just yet, but if you've got to be among the first to know, hit up the source link below.
If you've seen Ice Cream Sandwich and the GalaxyNexus in action, then it should be clear that the menu button has no future in the Android ecosystem. In order to drive that point home, Google has posted over at the Android Developer blog urging app creators to "say goodbye to the menu button." With the until now standard key getting the boot, big G wants devs to start designing interfaces that focus on the ActionBar introduced with Honeycomb. Of course, there's only so much room on the screen, and that's where the "action overflow" button comes in handy. Those vertical elipsis hide useful, but perhaps secondary options, that don't fit in the action bar. It also pops up on the far right of the navigation bar as a replacement to the menu button... basically because it behaves the same as menu, just in a different location. If nothing else at least Google is pushing Android and its apps towards a more uniform design. Check out the source for more details.
SUMO-snipping protein plays crucial role in T and B cell developmentPublic release date: 27-Jan-2012 [ | E-mail | Share ]
Contact: Scott Merville smerville@mdanderson.org 713-792-0661 University of Texas M. D. Anderson Cancer Center
SENP1 prevents crucial gene-activator STAT5 from becoming trapped in nucleus
HOUSTON - When SUMO grips STAT5, a protein that activates genes, it blocks the healthy embryonic development of immune B cells and T cells unless its nemesis breaks the hold, a research team led by scientists at The University of Texas MD Anderson Cancer Center reports today in Molecular Cell.
"This research extends the activity of SUMO and the Sentrin/SUMO-specific protease 1 (SENP1) to the field of immunology, in particular the early lymphoid development of T and B cells," said the study's senior author, Edward T. H. Yeh, M.D., professor and chair of MD Anderson's Department of Cardiology.
SUMO proteins, also known as the small ubiquitin-like modifiers or Sentrin, attach to other proteins in cells to modify their function or to move them within a cell. SENP1 is one of a family of six proteins that snips SUMO off of SUMO-modified proteins. SUMOylation (SUMO modification) of proteins has been implicated in development of cancer, heart and neurodegenerative diseases, among others.
The team first analyzed the role of SENP1 in the development of lymphoids in mice and found it is heavily expressed in precursor cells, the early stages of B and T cell development.
Working with genetically modified mice they developed that lack SENP1 gene expression, Yeh and colleagues found the mouse embryos had severe defects in their T and B cells, white blood cell lymphocytes that identify and fight infection.
SUMO pins STAT5 in the nucleus
Subsequent experiments led them to STAT5, a transcription factor known to play critical roles in the development and function of immune cells. Transcription factors work in the cell nucleus, activating gene expression by connecting to a gene's promoter region.
"STAT5 works in a cycle, moving from the cytosol of a cell into the nucleus to activate genes and then back out to the cytosol," Yeh said. "We found that when STAT5 is SUMOylated in the nucleus it gets trapped there when there's no SENP1 to remove SUMO."
The team found that SUMO muscles in on two other signaling events that govern STAT5 activity - phosphorylation and acetylation.
SUMO inhibits STAT5 signaling
STAT5 is activated in the cell cytosol when the JAK tyrosine kinase attaches a phosphate group at a specific site on the STAT5 protein. This transformed STAT5 crosses the nuclear membrane into the nucleus to transcribe genes.
The team found that SUMO attaches to STAT5 close to its phosphorylation site and that cells lacking SENP1 have increased SUMOylation and decreased phosphorylation.
SUMOylation vs. acetylation
In addition to phosphorylation, acetylation of STAT5 has been shown to be essential for STAT5 to cross the nuclear membrane into the nucleus to enhance gene transcription. Yeh and colleagues found that SUMO competes directly with acetyl groups for the same binding site, inhibiting acetylation.
"Without SENP1 to remove SUMO, STAT5 can't be acetylated or phosphorylated and can't be recycled for use again," Yeh said. "We discovered that SENP1 controls lymphoid development through regulation of SUMOylation of STAT5."
Since Yeh's lab discovered SUMOylation in 1996, SUMO has been found to alter the function of thousands of proteins.
Yeh is hosting the 6th International Conference SUMO, Ubiquitin, UBL Proteins: Implications for Human Diseases Feb. 8-11 in the Dan L. Duncan Building at MD Anderson. Yeh organizes the meeting every other year.
"There used to be so little known about SUMO. Now, a protein is assumed to be SUMOylated until proved otherwise," Yeh said.
###
Co-authors with Yeh are lead author Thang Van Nguyen, Ph.D., and Hong Dou of MD Anderson's Department of Cardiology; Pornpimon Angkasekwinai, Ph.D., and Chen Dong, Ph.D., of MD Anderson's Department of Immunology; Feng-Ming Lin, Ph.D., Long-Sheng Lu, M.D., Ph.D., and Jinke Cheng, D.V.M., of the Texas Heart Institute/St. Luke's Episcopal Hospital in Houston; and Y. Eugene Chin, Ph.D., of Brown University School of Medicine and Rhode Island Hospital.
Nguyen developed this project as a graduate student in The University of Texas Graduate School of Biomedical Sciences, a joint operation of MD Anderson and The University of Texas Health Science Center at Houston. Angkasekwinai also is affiliated with Thammasat University in Pathumthani, Thailand.
This research was funded by a grant from the National Cancer Institute and a fellowship to Nguyen from the Vietnam Education Foundation.
About MD Anderson
The University of Texas MD Anderson Cancer Center in Houston ranks as one of the world's most respected centers focused on cancer patient care, research, education and prevention. MD Anderson is one of only 40 comprehensive cancer centers designated by the National Cancer Institute. For eight of the past 10 years, including 2011, MD Anderson has ranked No. 1 in cancer care in "Best Hospitals," a survey published annually in U.S. News & World Report.
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AAAS and EurekAlert! are not responsible for the accuracy of news releases posted to EurekAlert! by contributing institutions or for the use of any information through the EurekAlert! system.
SUMO-snipping protein plays crucial role in T and B cell developmentPublic release date: 27-Jan-2012 [ | E-mail | Share ]
Contact: Scott Merville smerville@mdanderson.org 713-792-0661 University of Texas M. D. Anderson Cancer Center
SENP1 prevents crucial gene-activator STAT5 from becoming trapped in nucleus
HOUSTON - When SUMO grips STAT5, a protein that activates genes, it blocks the healthy embryonic development of immune B cells and T cells unless its nemesis breaks the hold, a research team led by scientists at The University of Texas MD Anderson Cancer Center reports today in Molecular Cell.
"This research extends the activity of SUMO and the Sentrin/SUMO-specific protease 1 (SENP1) to the field of immunology, in particular the early lymphoid development of T and B cells," said the study's senior author, Edward T. H. Yeh, M.D., professor and chair of MD Anderson's Department of Cardiology.
SUMO proteins, also known as the small ubiquitin-like modifiers or Sentrin, attach to other proteins in cells to modify their function or to move them within a cell. SENP1 is one of a family of six proteins that snips SUMO off of SUMO-modified proteins. SUMOylation (SUMO modification) of proteins has been implicated in development of cancer, heart and neurodegenerative diseases, among others.
The team first analyzed the role of SENP1 in the development of lymphoids in mice and found it is heavily expressed in precursor cells, the early stages of B and T cell development.
Working with genetically modified mice they developed that lack SENP1 gene expression, Yeh and colleagues found the mouse embryos had severe defects in their T and B cells, white blood cell lymphocytes that identify and fight infection.
SUMO pins STAT5 in the nucleus
Subsequent experiments led them to STAT5, a transcription factor known to play critical roles in the development and function of immune cells. Transcription factors work in the cell nucleus, activating gene expression by connecting to a gene's promoter region.
"STAT5 works in a cycle, moving from the cytosol of a cell into the nucleus to activate genes and then back out to the cytosol," Yeh said. "We found that when STAT5 is SUMOylated in the nucleus it gets trapped there when there's no SENP1 to remove SUMO."
The team found that SUMO muscles in on two other signaling events that govern STAT5 activity - phosphorylation and acetylation.
SUMO inhibits STAT5 signaling
STAT5 is activated in the cell cytosol when the JAK tyrosine kinase attaches a phosphate group at a specific site on the STAT5 protein. This transformed STAT5 crosses the nuclear membrane into the nucleus to transcribe genes.
The team found that SUMO attaches to STAT5 close to its phosphorylation site and that cells lacking SENP1 have increased SUMOylation and decreased phosphorylation.
SUMOylation vs. acetylation
In addition to phosphorylation, acetylation of STAT5 has been shown to be essential for STAT5 to cross the nuclear membrane into the nucleus to enhance gene transcription. Yeh and colleagues found that SUMO competes directly with acetyl groups for the same binding site, inhibiting acetylation.
"Without SENP1 to remove SUMO, STAT5 can't be acetylated or phosphorylated and can't be recycled for use again," Yeh said. "We discovered that SENP1 controls lymphoid development through regulation of SUMOylation of STAT5."
Since Yeh's lab discovered SUMOylation in 1996, SUMO has been found to alter the function of thousands of proteins.
Yeh is hosting the 6th International Conference SUMO, Ubiquitin, UBL Proteins: Implications for Human Diseases Feb. 8-11 in the Dan L. Duncan Building at MD Anderson. Yeh organizes the meeting every other year.
"There used to be so little known about SUMO. Now, a protein is assumed to be SUMOylated until proved otherwise," Yeh said.
###
Co-authors with Yeh are lead author Thang Van Nguyen, Ph.D., and Hong Dou of MD Anderson's Department of Cardiology; Pornpimon Angkasekwinai, Ph.D., and Chen Dong, Ph.D., of MD Anderson's Department of Immunology; Feng-Ming Lin, Ph.D., Long-Sheng Lu, M.D., Ph.D., and Jinke Cheng, D.V.M., of the Texas Heart Institute/St. Luke's Episcopal Hospital in Houston; and Y. Eugene Chin, Ph.D., of Brown University School of Medicine and Rhode Island Hospital.
Nguyen developed this project as a graduate student in The University of Texas Graduate School of Biomedical Sciences, a joint operation of MD Anderson and The University of Texas Health Science Center at Houston. Angkasekwinai also is affiliated with Thammasat University in Pathumthani, Thailand.
This research was funded by a grant from the National Cancer Institute and a fellowship to Nguyen from the Vietnam Education Foundation.
About MD Anderson
The University of Texas MD Anderson Cancer Center in Houston ranks as one of the world's most respected centers focused on cancer patient care, research, education and prevention. MD Anderson is one of only 40 comprehensive cancer centers designated by the National Cancer Institute. For eight of the past 10 years, including 2011, MD Anderson has ranked No. 1 in cancer care in "Best Hospitals," a survey published annually in U.S. News & World Report.
[ | E-mail | Share ]
?
AAAS and EurekAlert! are not responsible for the accuracy of news releases posted to EurekAlert! by contributing institutions or for the use of any information through the EurekAlert! system.
First time accepted submitter AbilityLiving writes "Two high schoolers have launched a Lego Man to 80,000 feet ? three times the height of a jet ? in a homebrew project that involved a few Ebay-purchased cameras, a giant helium balloon and a star-ship full of ingenuity."
On April 8th, 2010, I watched helplessly as the only oxygen machine in a poorly equipped Haitian clinic was taken from a premature baby and given to a woman struggling in labor. The woman gave birth to a healthy girl named Rodsandy. The premature baby died; he had no name.
Now, almost two years later, a stunning, modern teaching hospital with oxygen outlets in the walls is about to open in the town of Mirebalais thanks to a joint effort between Partners In Health, the government of Haiti, and donors from all over the world. Earlier this month, Dr. Paul Farmer (co-founder of Partners In Health) and Dr. David Walton (director of the hospital) took me on a tour of the 320-bed facility. At the very end of this video, Paul pours out his heart in the most succinct, passionate vision of health care equity I have ever heard.
Our intrepid reporters have been busy at the Sundance Film Festival, trekking through the snow to bring you the latest news in all things movies. (Suckers!) Meanwhile, the rest of us have been staying cozy at home, and getting ready for the awesome horror slate that 2012 seems to be promising.
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Public release date: 27-Jan-2012
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