R N Bohnsack

Department of Biochemistry, Medical College of Wisconsin, 8701 W. Watertown Plank Rd., Milwaukee, WI, 53226, USA.

16 publications 1996 – 2024

What does R N Bohnsack research?

Dr. Bohnsack studies how specific proteins in cells can help protect insulin-producing beta cells from damage caused by saturated fats, such as palmitate. When these cells are damaged, they can lose their ability to produce insulin, which is crucial for regulating blood sugar levels. The researcher looks closely at a protein called Cation-Independent Mannose 6-Phosphate Receptor (CI-MPR), which plays a key role in managing cellular waste and protecting these important cells from harm. By understanding these mechanisms, their work could lead to new strategies for treating type 2 diabetes.

Key findings

  • Insulin-producing cells with the CI-MPR protein are protected from palmitate damage, while those without it show significant vulnerability.
  • Cells lacking CI-MPR experience much more damage and impaired insulin production, indicating its critical protective role.
  • The discovery opens up pathways for developing treatments that enhance the waste-disposal process in cells, potentially leading to better management of type 2 diabetes.

Frequently asked questions

Does Dr. Bohnsack study diabetes?
Yes, Dr. Bohnsack's research focuses on understanding how to protect insulin-producing cells, which is directly relevant to diabetes treatment.
What specific proteins does Dr. Bohnsack research?
Dr. Bohnsack researches the Cation-Independent Mannose 6-Phosphate Receptor (CI-MPR) and its role in protecting beta cells from damage.
How is Dr. Bohnsack's work relevant for type 2 diabetes patients?
Their findings could lead to new therapies aimed at preserving insulin production in patients suffering from type 2 diabetes.

Publications in plain English

Lysosomal enzyme binding to the cation-independent mannose 6-phosphate receptor is regulated allosterically by insulin-like growth factor 2.

2024

Scientific reports

Bohnsack RN, Misra SK, Liu J, Ishihara-Aoki M, Pereckas M +4 more

Plain English
This study looked at how a protein called the cation-independent mannose 6-phosphate receptor (CI-MPR) interacts with lysosomal enzymes and the hormone insulin-like growth factor 2 (IGF2). The researchers found that IGF2 changes the shape of CI-MPR, which prevents it from binding to lysosomal enzymes effectively. This is important because understanding these interactions can help in treating lysosomal storage diseases, where enzyme delivery is crucial for patient health. Who this helps: This benefits patients with lysosomal storage diseases who need effective treatments.

PubMed

Tissue plasminogen activator is a ligand of cation-independent mannose 6-phosphate receptor and consists of glycoforms that contain mannose 6-phosphate.

2021

Scientific reports

Miller JJ, Bohnsack RN, Olson LJ, Ishihara M, Aoki K +2 more

Plain English
This study looked at how tissue plasminogen activator (tPA), a protein important for breaking down blood clots, interacts with a specific receptor (CI-MPR) in the body. The researchers found that tPA binds to CI-MPR with a strong affinity and that this interaction is influenced by a sugar molecule called mannose 6-phosphate (M6P) present on tPA. These findings could be significant because they enhance our understanding of how tPA works and may lead to improved treatments for conditions related to blood clots. Who this helps: This helps patients who are at risk for blood clotting disorders.

PubMed

Cation-Independent Mannose 6-Phosphate Receptor Deficiency Enhances β-Cell Susceptibility to Palmitate.

2018

Molecular and cellular biology

Baldwin AC, Naatz A, Bohnsack RN, Bartosiak JT, Oleson BJ +3 more

Plain English
Researchers discovered that insulin-producing cells protect themselves from damage caused by palmitate (a common fatty acid) by using a cellular cleanup system called lysosomes to break down and remove damaged proteins. Cells that lacked a specific protein needed to deliver garbage to lysosomes were much more vulnerable to palmitate damage, while cells with this protein intact survived better. This finding suggests that keeping the lysosomal cleanup system working properly is essential for pancreatic cells to survive when exposed to excess fat.

PubMed

Expression of insulin-like growth factor 2 receptor in corneal keratocytes during differentiation and in response to wound healing.

2014

Investigative ophthalmology & visual science

Bohnsack RN, Warejcka DJ, Wang L, Gillespie SR, Bernstein AM +2 more

Plain English
This study looked at a protein called the insulin-like growth factor 2 receptor (IGF2R) in cells from the cornea, the clear front part of the eye. Researchers found that IGF2R levels increased significantly during corneal healing—by about 11 times in wounded areas—suggesting it plays an important role in this process. Understanding how IGF2R affects healing can help improve treatments for corneal injuries. Who this helps: This helps patients with corneal injuries and doctors treating eye conditions.

PubMed

Glycosylation-independent lysosomal targeting of acid α-glucosidase enhances muscle glycogen clearance in pompe mice.

2013

The Journal of biological chemistry

Maga JA, Zhou J, Kambampati R, Peng S, Wang X +7 more

Plain English
This study looked at a new way to deliver an enzyme called acid α-glucosidase (GAA) to help clear excess glycogen in the muscles of mice with Pompe disease. By attaching a special tag (GILT) to the enzyme, researchers found that it was absorbed by muscle cells 25 times better than the standard version of the enzyme. This improved delivery resulted in a significantly better ability to reduce glycogen buildup in the muscles, making it a promising option for treating Pompe disease. Who this helps: This benefits patients with Pompe disease who need better treatment options.

PubMed

Intermonomer interactions are essential for lysosomal enzyme binding by the cation-dependent mannose 6-phosphate receptor.

2010

Biochemistry

Olson LJ, Sun G, Bohnsack RN, Peterson FC, Dahms NM +1 more

Plain English
This study looked at the cation-dependent mannose 6-phosphate receptor (CD-MPR), which helps transport important enzymes to lysosomes inside cells. Researchers found that when they made a specific change to the receptor, it significantly decreased its ability to bind to these enzymes—specifically, it was 60% less effective at binding compared to the normal receptor. This matters because understanding how the CD-MPR works can help improve treatments for diseases related to enzyme delivery dysfunction. Who this helps: This helps doctors and researchers working on treatments for lysosomal storage diseases.

PubMed

Residues essential for plasminogen binding by the cation-independent mannose 6-phosphate receptor.

2010

Biochemistry

Bohnsack RN, Patel M, Olson LJ, Twining SS, Dahms NM

Plain English
This study focused on how a particular protein called the cation-independent mannose 6-phosphate receptor (CI-MPR) binds to plasminogen, a protein involved in breaking down blood clots. Researchers found that two specific parts (lysine residues) of the CI-MPR are crucial for this binding; namely, Lys53 and Lys125, which help the receptor recognize plasminogen effectively. The ability to understand this interaction is important because it could lead to better treatments for conditions related to blood clotting. Who this helps: This helps patients at risk of blood clot-related issues and their healthcare providers.

PubMed

Structural basis for recognition of phosphodiester-containing lysosomal enzymes by the cation-independent mannose 6-phosphate receptor.

2010

Proceedings of the National Academy of Sciences of the United States of America

Olson LJ, Peterson FC, Castonguay A, Bohnsack RN, Kudo M +4 more

Plain English
This study looked at how a specific receptor in our cells (the cation-independent mannose 6-phosphate receptor, or CI-MPR) recognizes certain enzymes that are important for breaking down materials in lysosomes, the cell's waste disposal units. Researchers found that domain 5 of the CI-MPR has a unique structure that allows it to recognize these enzymes, even when some of them are not fully matured, meaning they can still get to the lysosomes effectively. Understanding this process is crucial because it helps ensure that important enzymes reach their destination, which is vital for normal cell function and development. Who this helps: This benefits patients with lysosomal storage disorders and their doctors.

PubMed

Cation-independent mannose 6-phosphate receptor: a composite of distinct phosphomannosyl binding sites.

2009

The Journal of biological chemistry

Bohnsack RN, Song X, Olson LJ, Kudo M, Gotschall RR +4 more

Plain English
This study looked at a protein called the cation-independent mannose 6-phosphate receptor (CI-MPR) that helps transport important enzymes to the lysosomes in cells. Researchers found that the CI-MPR has three different sites that can recognize specific sugar structures; one of these sites (domain 5) can bind about 60 times better when it works alongside another site (domain 3). Understanding how these sites work together is crucial because it helps clarify how cells manage and deliver these enzymes, which is important for many bodily functions. Who this helps: This benefits researchers and doctors working on treatments for lysosomal storage diseases.

PubMed

Domain 5 of the cation-independent mannose 6-phosphate receptor preferentially binds phosphodiesters (mannose 6-phosphate N-acetylglucosamine ester).

2007

Biochemistry

Chavez CA, Bohnsack RN, Kudo M, Gotschall RR, Canfield WM +1 more

Plain English
This study focused on a specific part of a receptor, called domain 5 of the cation-independent mannose 6-phosphate receptor (CI-MPR), to see how well it binds to certain sugar-like molecules that help direct enzymes to the cell's waste disposal system. The research found that domain 5 binds 14 to 18 times more strongly to a specific type of sugar called mannose 6-phosphate N-acetylglucosamine ester than to another type called mannose 6-phosphate, suggesting that this domain is important for acknowledging these sugars and helping with enzyme delivery. This discovery helps enhance our understanding of how enzymes are transported within cells, which could lead to better treatments for conditions related to enzyme deficiencies. Who this helps: This benefits patients with enzyme-related disorders and the doctors treating them.

PubMed

Pleiotropic effects of ATP.Mg2+ binding in the catalytic cycle of ubiquitin-activating enzyme.

2006

The Journal of biological chemistry

Tokgöz Z, Bohnsack RN, Haas AL

Plain English
This study focused on understanding how certain changes in a key enzyme, called HsUba1a, affect its ability to activate a protein called ubiquitin, which plays a crucial role in regulating various cellular functions. Researchers found that specific mutations in the enzyme significantly weaken its ability to bind ATP, which is vital for its activity, leading to a reduced efficiency in forming necessary enzyme complexes. This matters because these findings reveal important details about how mutations can disrupt the function of enzymes related to protein regulation, which could impact diseases linked to protein breakdown. Who this helps: This helps researchers and medical professionals understand enzyme functions better, potentially leading to new treatments for diseases caused by protein regulation issues.

PubMed

Protein interactions within the N-end rule ubiquitin ligation pathway.

2003

The Journal of biological chemistry

Siepmann TJ, Bohnsack RN, Tokgöz Z, Baboshina OV, Haas AL

Plain English
This study looked at how proteins interact in a specific pathway involved in tagging proteins for degradation using a molecule called ubiquitin. Researchers found that certain proteins showed strong binding at very low concentrations (around 100 nanomoles), and that the way these proteins bind is essential for the process, with only half the binding strength affecting how well the tagging happens. Understanding these interactions is important because they help clarify how cells regulate protein destruction, which has implications for various diseases linked to protein mismanagement. Who this helps: This helps researchers and doctors working on diseases related to protein degradation, like cancer and neurodegenerative disorders.

PubMed

Conservation in the mechanism of Nedd8 activation by the human AppBp1-Uba3 heterodimer.

2003

The Journal of biological chemistry

Bohnsack RN, Haas AL

Plain English
This study focused on a specific enzyme in humans called AppBp1-Uba3, which activates a protein called Nedd8. The researchers found that this enzyme works efficiently, with a rate of 3.5 reactions per second, and it has similar properties to another enzyme involved in protein activation, Uba1. Understanding how AppBp1-Uba3 functions is important because it helps us learn more about protein regulation in cells, which can impact diseases like cancer. Who this helps: This helps researchers and doctors working on cancer treatments and other diseases related to protein regulation.

PubMed

Kinetic analysis of the conjugation of ubiquitin to picornavirus 3C proteases catalyzed by the mammalian ubiquitin-protein ligase E3alpha.

2001

The Journal of biological chemistry

Lawson TG, Sweep ME, Schlax PE, Bohnsack RN, Haas AL

Plain English
This study looked at how a protein called ubiquitin attaches to specific viral proteins (3C proteases) associated with the encephalomyocarditis virus and hepatitis A virus. The researchers found that these viral proteins can be tagged with ubiquitin at different rates, with the encephalomyocarditis virus 3C protease attaching to it at a maximum rate of 0.051 pmol/min, while the hepatitis A virus version reached 0.018 pmol/min. Understanding this process is important because it reveals how viruses can evade destruction by the host's immune system, which could help in developing treatments. Who this helps: This helps doctors and researchers working on antiviral therapies.

PubMed

Site-directed mutagenesis using positive antibiotic selection.

1997

Molecular biotechnology

Bohnsack RN

Plain English
This study looked at a method for changing specific parts of DNA in a lab setting, which is important for genetic research. Researchers found that using a combination of two special pieces of DNA allowed them to successfully make these changes in 60 to 90% of cases. This matters because it offers an effective way to introduce targeted mutations, which can help in various applications, including developing new treatments. Who this helps: This helps researchers working on genetic therapies and drug development.

PubMed

Site-directed mutagenesis using positive antibiotic selection.

1996

Methods in molecular biology (Clifton, N.J.)

Bohnsack RN

PubMed

Publication data sourced from PubMed . Plain-English summaries generated by AI. Not medical advice.