Major Research Interests: Cellular Functions of GLUT1CBP(GIPC). Historically, my laboratory has been interested in identifying structural domains and protein interactions that confer the characteristic transport kinetics, membrane targeting, and insulin responsiveness that differentiate the behavior of the homologous glucose transporters. Recently, we identified a unique GLUT1 C-terminal binding protein GLUT1CBP (also termed GIPC) which contains a PDZ domain that recognizes and binds to the C-terminal four amino acids of GLUT1. Among the known protein-protein interactions for GLUT1CBP, a key functional interaction which we have discovered is the ability of its C-terminus to bind to the globular tail of myosin VI. We have refined the location of the domains that interact in myosin VI and GLUT1CBP (model) and have demonstrated that the movement of the GLUT1CBP complex is: a)microtubule independent (video1), and b)actin dependent (video 2). In addition, complexes of GLUT1CBP and myosin VI can be observed to move coordinately in a direction consistent with myosin VI coupled movement (video 3).

The number of proteins identified by ours and other laboratories that interact with the PDZ domain of GLUT1CBP are numerous enough to implicate GLUT1CBP as an important adapter protein linking diverse cargos (including GLUT1) bound by the PDZ domain to cellular movement and targeting via the atypical motor protein myosin VI. This would suggest that one of several potential cellular functions for GLUT1CBP is to provide an important protein/vesicle targeting and/or anchoring role for proteins that bind to its PDZ domain (model).

Thus our current efforts are focused upon examining the function of GLUT1CBP in regulating the distribution and movement of GLUT1 and other interacting proteins within the cell. As several of the newly identified interacting proteins comprise important pathways that regulate cell adhesion, cell division, motility, and the availability of sugar as an energy source for the cell, our laboratory also wishes to determine, through a better understanding of GLUT1CBP’s potential function in protein trafficking, whether a means to control its function can be utilized to influence or alter one or more aspects of cell mobility, adhesion, or proliferation that ultimately affect tumor progression and survival.

GLUT1CBP(GIPC): An Adapter Protein Interacting with Myosin VI: The illustration presents the proposed adapter function for GLUT1CBP(GIPC), linking potential cargo proteins to myosin VI-catalyzed movement along F-actin filaments. The C termini of GLUT1 or other potential vesicle bound cargo proteins (yellow) bind to the N-terminal region of the PDZ domain (red) of GLUT1CBP(GIPC). This complex interacts with myosin VI through a C-terminal domain of GLUT1CBP(GIPC) and a central domain in the tail of myosin VI (blue). Both interacting domains are marked by white boxes. A potential secondary interaction domain in GLUT1CBP(GIPC) is marked with a dotted rectangle. The motor domain (green) of myosin VI catalyzes movement of the complex toward the negative end of the F-actin filament. A gray box marks the region containing the proline repeats in the N-terminus of GLUT1CBP(GIPC). Numbers represent the amino acid residues within GLUT1CBP(GIPC) and in myosin VI that are representative of the corresponding residues of the full-length GLUT1CBP(GIPC) and pig myosin VI molecules. The two C-terminal inserts present in variant forms of myosin VI are not shown.

Support for this model is presented in three videos below.

Dependence of GLUT1CBP(GIPC) movement on intact F-actin filaments: The movement of GFP-GLUT1CBP along filaments within cellular extensions is blocked when F-actin filaments are disrupted by the addition of cytochalasin D (added at 6 min) as predicted by the model.

A further requirement of the model would be that if GLUT1CBP(GIPC) movement is mediated by myosin VI, then both should co-localize and move together as a complex. This is illustrated in the next video.

Myosin VI and GLUT1CBP(GIPC) move co-ordintely along actin filaments. Consistent with myosin VI catalyzed movement, YFP-GLUT1CBP and CFP-myosin VI co-localize and move together towards the negative end of the actin filament consistent with the myosin VI adapter function proposed in the model.

Selected Publications

1. Influenza A (H3) Outbreak at a Hurricane Harvey Megashelter in Harris County, Texas: Successes and Challenges in Disease Identification and Control Measure Implementation. Liu L, Haynie A, Jin S, Zangeneh A, Bakota E, Hornstein BD, Beckham D, Reed BC, Kiger J, McClendon M, Perez E, Schaffer M, Becker L, Shah UA. Disaster Med Public Health Prep. 2019 Feb;13(1):97-101. doi: 10.1017/dmp.2018.159. PMID: 30841952

2. Association of exhaled nitric oxide with ethnicity and sex in rural Georgia youth. Reed BC, Waller JL, Ownby DR, Tingen MS. Ann Allergy Asthma Immunol. 2019 Mar;122(3):333-334.e1. doi: 10.1016/j.anai.2018.12.011. Epub 2018 Dec 14. No abstract available. PMID: 30557616

3. Shifting microbial communities sustain multiyear iron reduction and methanogenesis in ferruginous sediment incubations. Bray MS, Wu J, Reed BC, Kretz CB, Belli KM, Simister RL, Henny C, Stewart FJ, DiChristina TJ, Brandes JA, Fowle DA, Crowe SA, Glass JB. Geobiology. 2017 Sep;15(5):678-689. doi: 10.1111/gbi.12239. Epub 2017 Apr 17. PMID: 28419718

4. Geriatric Care Issues: An American and an International Perspective. Sidani MA, Reed BC, Steinbauer J. Prim Care. 2017 Mar;44(1):e15-e36. doi: 10.1016/j.pop.2016.09.018. Review. PMID: 28164825

5. Inform patients about delays. Reed BC. Fam Pract Manag. 2016 Sep-Oct;23(5):47. No abstract available. PMID: 27626123 Free Article

6. Incorporating Cultural Sensitivity into Interactive Entertainment-Education for Diabetes Self-Management Designed for Hispanic Audiences. Kline KN, Montealegre JR, Rustveld LO, Glover TL, Chauca G, Reed BC, Jibaja-Weiss ML. J Health Commun. 2016 Jun;21(6):658-68. doi: 10.1080/10810730.2016.1153758. Epub 2016 May 11. PMID: 27166651

7. An Assessment of Coliform Bacteria in Water Sources Near Appalachian Trail Shelters Within the Great Smoky Mountains National Park. Reed BC, Rasnake MS. Wilderness Environ Med. 2016 Mar;27(1):107-10. doi: 10.1016/j.wem.2015.09.019. Epub 2015 Dec 7. PMID: 26674141

8. CPEB1 promotes differentiation and suppresses EMT in mammary epithelial cells. Grudzien-Nogalska E, Reed BC, Rhoads RE. J Cell Sci. 2014 May 15;127(Pt 10):2326-38. doi: 10.1242/jcs.144956. Epub 2014 Mar 14. PMID: 24634508 Free PMC Article

9. Dematin and adducin provide a novel link between the spectrin cytoskeleton and human erythrocyte membrane by directly interacting with glucose transporter-1. Khan AA, Hanada T, Mohseni M, Jeong JJ, Zeng L, Gaetani M, Li D, Reed BC, Speicher DW, Chishti AH. J Biol Chem. 2008 May 23;283(21):14600-9. doi: 10.1074/jbc.M707818200. Epub 2008 Mar 17. PMID: 18347014 Free PMC Article

10. Chemiluminescent optical fiber immunosensor for detection of autoantibodies to ovarian and breast cancer-associated antigens. Salama O, Herrmann S, Tziknovsky A, Piura B, Meirovich M, Trakht I, Reed B, Lobel LI, Marks RS. Biosens Bioelectron. 2007 Feb 15;22(7):1508-16. Epub 2006 Aug 9. PMID: 16904309

Complete List of my Published Work: Bibliography
 

Post-doctoral Fellows

While we are not currently recruiting Post-doctoral Fellows, quality candidates will always be considered.  To enquire about opportunities, contact Dr. Reed at breed@lsuhsc.edu.

Graduate Students

Graduate students interested in conducting research in the Orr lab should review the current laboratory research directions and contact Dr. Reed at breed@lsuhsc.edu.

Undergraduate Research Assistants

We are not currently hiring any additional undergraduates. However, positions can become available during the summer.