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Katherine (Kathy) Wilson, Ph.D.

Katherine (Kathy) Wilson, Ph.D.

Academic Titles: 
Position Title: 
Principal Investigator
410-955-1801 (Office)
410-614-2654 (Lab)
410-955-4129 (Fax)

Department of Cell Biology
Johns Hopkins University School of Medicine
725 N. Wolfe Street, G10 WBSB
Baltimore, MD 21205

Within each human cell is a NUCLEUS, 'mothership' of the human genome and still the least-understood cellular structure. Chromosomes are enclosed by the nuclear envelope (NE) and communicate with the cytoplasm through Nuclear Pore Complexes (NPCs). The inner and outer membranes of the NE are mechanically connected by SUN-domain proteins and nesprins, which form LINC (links the nucleoskeleton and cytoskeleton) complexes. LINC complexes are anchored to nuclear intermediate filament (nuclear ‘lamina’) networks. Together the NE and nuclear lamina protect, organize and help regulate chromatin.

Research in the Wilson lab centers on the three key components of nuclear lamina structure: lamins (encoded by LMNA, LMNB1, LMNB2), LEM-domain proteins (e.g., emerin, encoded by EMD), and BAF (Barrier to autointegration factor, encoded by BANF1). These proteins all bind each other directly, and are collectively required to organize and regulate chromatin, efficiently segregate chromosomes and rebuild nuclear structure after mitosis. Mutations in these proteins cause human ‘laminopathy’ diseases including Emery-Dreifuss muscular dystrophy (EDMD), cardiomyopathy, neuropathy, ‘accelerated aging’ (progeria syndromes), lipodystrophy/diabetes and metabolic syndrome. These disease mechanisms are not understood.

Current work aims to understand the molecular mechanisms of emerin function at the nuclear envelope, emerin molecular attachments to BAF/chromatin and lamin filaments, and how these interactions are controlled by metabolic status (O-GlcNAc cycle), phosphorylation, mechanical force and cell signaling. 

Kathy Wilson on the Structure of the Nucleus:
YouTube Video

Recent Lab Members Include:

Jason Berk, Ph.D.
Postdoctoral Fellow w/Mark Hochstrasser
Yale University

Hemanshi Chawla
Ph.D. Student at UMBC

Dan Simon, Ph.D.
Postdoctoral Fellow w/Michael Rout
Rockefeller University


Research Interest: 
Nuclear envelope, lamins and nucleoskeleton; Emery-Dreifuss muscular dystrophy

The cell nucleus surrounds, organizes and mechanically protects the genome. Lamin filament networks and nuclear membrane proteins support and influence most activities in the nucleus, with central and dynamic roles in customizing the 3D spatial organization of individual chromosomes needed for tissue-specific gene silencing. The functions and regulation of nuclear ‘lamina’ networks are an open frontier in biology.

Selected Publications:
Crews DC, Wilson KL, Sohn J, Kabacoff CM, Poynton SL, Murphy LR, Bolz J, Wolfe A, White PT, Will C, Collins C, Gauda E, Robinson DN*. Helping scholars overcome socioeconomic barriers to medical and biomedical careers: Creating a pipeline initiative.  Teach. Learn. Med. 2020; 1-12. DOI: 10.1080/10401334.2020.1729161.  
Arun A, Eddings CR and Wilson KL (2019) Novel missense alleles of SIGMAR1 as tools to understand emerin-dependent gene silencing in response to cocaine. Exp. Biology & Medicine (in press) 
Dharmaraj T, Guan YC, Liu J, Badens C, Gaborit B and Wilson KL (2019) Rare BANF1 variants and relatively frequent EMD variants including ‘healthy lipid’ emerin p.D149H in the ExAC cohort. Front. Cell Dev. Biol. 05 April 2019 https://doi.org/10.3389/fcell.2019.00048  
Wilson KL (2018) Nuclear import pathway key to rescuing dominant progerin phenotypes. Science Signaling 11(537). pii: eaat9448    
Simon DN, Wriston A, Florwick A, Fan Q, Dharmaraj T, Shabanowitz J, Peterson SB, Gruenbaum Y, Carlson CR, Gronning-Wang LM, Hunt DF and Wilson KL (2018) OGT (O-GlcNAc transferase) selectively modifies multiple residues unique to lamin A. Cells 7:44  
Dharmaraj T and Wilson KL. (2017). How chromosomes unite. Nature 551:568-569.
Florwick A, Dharmaraj T, Jurgens J, Valle D, Wilson KL. 2017.  LMNA sequences of 60,706 unrelated individuals reveal 132 novel missense variants in A-type lamins and suggest a link between variant p.G602S and Type 2 Diabetes.  Jun 15;8:79. doi: 10.3389/fgene.2017.00079. eCollection 2017.
Sonnenberg A and Wilson KL (2016). Preface. Methods Enzymol. 569:xix-xx. [Co-Editor]
Berk JM and Wilson KL. (2016). Simple separation of functionally distinct populations of lamin-binding proteins. Methods Enzymol. 569:101-114.
Mojica SA, Hovis KM, Frieman MB, Tran B, Hsia RC, Ravel J, Jenkins-Houk C, Wilson KL, Bavoil PM (2015) SINC, a type III secreted protein of Chlamydia psittaci, targets the inner nuclear membrane of infected cells and uninfected neighbors. Molecular Biology of the Cell 26:1918-1934.
Berk JM, Simon DN, Jenkins-Houk CR, Westerbeck JW, Gronning-Wang LM, Carlson CR, Wilson KL (2014) The molecular basis of emerin-emerin and emerin-BAF interactions. J. Cell Science 127:3956-3969. 
Bar DZ, Davidovich M, Lamm AT, Zer H, Wilson KL and Gruenbaum Y (2014) BAF-1 mobility is regulated by environmental stresses. Molecular Biology of the Cell 25:1127-36. PMC3967975
Berk JM, Tifft KE and Wilson KL. (2013) The nuclear envelope LEM-domain protein emerin. Nucleus 4:1-17. 
Berk JM, Maitra S, Dawdy AW, Shabanowitz J, Hunt DJ and Wilson KL. (2013) O-GlcNAc regulates emerin binding to BAF in a chromatin- and lamin B-enriched ‘niche’. J. Biological Chemistry 288:30192-209.
Wozniak M, Baker BM, Chen C and Wilson KL. (2013) Emerin-binding transcription factor Lmo7 is regulated by association with p130Cas at focal adhesions. PeerJ e134
Simon DN and Wilson KL. (2013) Partners and posttranslational modifications of nuclear lamins. Chromosoma 122:13-31. 
Simon DN, Domaradzki T, Hofmann WA and Wilson KL. (2013) Lamin A tail modification by SUMO1 is disrupted by familial partial lipodystrophy-causing mutations. Molecular Biology of the Cell 24:342-50.
Barkan R, Zahand AJ, Sarabi K, Lamm AT, Feinstein N, Haithcock E, Wilson KL, Liu J and Gruenbaum Y. (2012) Ce-emerin and LEM-2: essential roles in Caenorhabditis elegans development, muscle function and mitosis. Molecular Biology of the Cell 23:543-552. 
Gjerstorff MF, Rösner HI, Pedersen CB, Greve KB, Schmidt S, Wilson KL, Mollenhauer J, Besir H, Poulsen FM, Møllegaard NE and Ditzel HJ. (2012) GAGE cancer-germline antigens are recruited to the nuclear envelope by germ cell-less (GCL). PloS One 7:e45819.
Simon DN and Wilson KL. (2011) The nucleoskeleton as a dynamic genome-associated ‘network of networks.’ Nature Reviews Mol. Cell. Biol. 12:695-708.
Montes de Oca RM, Andreassen PR and Wilson KL. (2011) Barrier to Autointegration Factor influences specific histone modifications. Nucleus 2:580-590. 
Wilson KL and Dawson SC. (2011) Functional evolution of nuclear structure. J Cell Biology 195:171-181.
Wilson KL and Berk JM. (2010) The nuclear envelope at a glance. J Cell Science 123:1973-1978. 
Simon DN, Zastrow MS, Wilson KL. (2010) Direct actin binding to A- and B-type lamin tails and actin filament bundling by the lamin A tail. Nucleus 1:264-272. 
Tifft KE, Bradbury KA and Wilson KL. (2009) Tyrosine phosphorylation of nuclear membrane protein emerin by Src, Abl and other kinases. J Cell Science 122:3780-3790. 
Montes de Oca R, Shoemaker CJ, Gucek M, Cole RN and Wilson KL. (2009) Barrier to Autointegration Factor proteome reveals chromatin-regulatory partners. PLoS One e7050. 
Holaska JM and Wilson KL. (2007) An emerin ‘proteome’: purification of distinct emerin-containing complexes from HeLa cells suggests molecular basis for diverse roles including gene regulation, mRNA splicing, signaling, mechanosensing and nuclear architecture. Biochemistry 46, 8897-908. 
Margalit A, Neufeld E, Feinstein N, Wilson KL, Podbilewicz B and Gruenbaum Y (2007).  Barrier to autointegration factor (BAF) blocks premature cell fusion and maintains adult muscle integrity in C. elegans. J Cell Biology 178:661-673. 
Zastrow MS, Flaherty DB, Benian GM and Wilson KL (2006). Nuclear titin interacts with A- and B-type lamins in vitro and in vivo. J. Cell Science 119:239-249.
Montes de Oca R, Lee KK and Wilson KL (2006). Binding of barrier-to-autointegration factor (BAF) to histone H3 and selected linker histones including H1.1.  J Biological Chemistry 280:42252-62