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Robert D. Goldman
Rank: Stephen Walter Ranson Professor and
Chair
Brief description of research area: Structure and Function of Cytoskeletal Systems
Degree: Ph.D.
Institution degree obtained from: Princeton University
Voice: 312.503.4215
Fax: 312.503.7912
E-mail: r-goldman@northwestern.edu
Detailed research description:
Our research focuses on the structure and function of cytoskeletal
systems, particularly the intermediate filament (IF) system in fibroblasts,
epithelial cells, and nerve cells. IFs are composed
of large families of proteins that vary in composition from one cell type to
another--even among cells in the same tissue. Using a variety of techniques,
we have demonstrated that IFs form elaborate
networks that course throughout the cytoplasm and establish connections with
both the nuclear and cell surfaces.
At the nuclear surface, they are linked either directly or indirectly with
the nuclear lamins, which are chromatin-associated
IF protein family members. At the level of the plasma membrane, IFs are involved as cytoskeletal
linkages to the focal adhesion of fibroblasts and the desmosomes
and hemidesmosomes of epithelial cells. Throughout
the cytoplasm, we have shown that IFs are
associated with the other cytoskeletal elements,
such as microtubules and microfilaments.
Our approach to studying
the IF system involves biochemical, morphological, immunological, cell
physiological, and molecular techniques. Our hypothesis is that the IF system
forms a continuous network linking the nuclear and cell surfaces, functioning
in such diverse activities as the establishment and maintenance of cell
shape, organelle movements within the cytoplasm, nuclear positioning,
nuclear-cytoplasmic interactions, and signal
transduction.
Since many human diseases have been linked to changes in cytoskeletal IF systems, we are also developing models to
study the mechanisms involved in IF alterations in various diseases. One
example is amyotrophic lateral sclerosis (ALS or Lou Gehrig's
disease) in which we have been able to induce neurofibrillary
tangles to form in single cultured nerve cells. These tangles are similar to
those found in ALS neurons. Therefore, we are able to study the effects of neurofilament tangle formation in single cells. During
the summer, researchers from this laboratory also conduct studies on the
mechanisms of chromatin/nuclear envelope interactions in eggs of the surf
clam at the Marine Biological Laboratory in Woods Hole.
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Representative
publications:
Sivaramakrishnan
S, Schneider JL, Sitikov A, Goldman RD
and Ridge KM. (2009) Shear stress induced reorganization of the keratin
intermediate filament network requires phosphorylation
of K18Ser33 via PKC z and 14-3-3. Mol Biol
Cell ;Apr 8: epub. PMID
19357195
Shimi
T, Pfleghaar K, Kojima SI, Pack CG, Solivei I, Goldman AE, Adam SA, Shumaker DK, Kinjo M, Cremer T and Goldman
RD. (2008) The A- and
B-type nuclear lamin networks: microdomains involved in chromatin organization and
transcription. Genes Dev 22:3409-3421. PMID 19141474 PMCID: PMC2607069
Shumaker DK, Solimando
L, Sengupta
K, Adam SA, Grunwald
A, Strelkov S, Aebi U, Cardoso MC and Goldman RD.
(2008) The Highly conserved nuclear lamin Ig-fold binds to PCNA: its role in DNA replication. J Cell Biol ;Apr 21;181(2):269-80. PMID 18426975 PMCID: PMC2315674
Adam SA, Sengupta
K and Goldman RD. (2008) Regulation of
nuclear lamin polymerization by importin α [alpha]. J Biol Chem;Mar 28;283:8462-8468. PMID 18227062 PMCID: PMC2417177
Sivaramakrishnan
SI, DeGiulio
JV, Lorand L, Goldman RD and Ridge KM. (2008) Micromechanical properties of
keratin intermediate filament networks. PNAS;Jan
22:105(3):889-894. PMID
18199836 PMCID: PMC2242724
Dechat
T, Shimi
T, Adam SA, Rusinol
A, Andres DA, Spielmann HP, Sinensky
MS and Goldman RD. (2007) Alterations in
mitosis and cell cycle progression caused by a mutant lamin
A known to accelerate human aging.
PNAS;104(12):4955-60. PMID
17360326 PMCID:
PMC1829246
Kural
C, Serpinskaya
AS, Chou YH, Goldman RD, Gelfand VI
and Selvin PR. (2007) Tracking melanosomes inside a cell to study their molecular
motors and their interaction.
PNAS ;104(13):5378-5382.
PMID 17369356 PMCID: PMC1838505
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