The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Pacsin 2 is recruited to caveolae and functions in caveolar biogenesis
Abstract
The pacsin (also termed syndapin) protein family is well characterised structurally. They contain F-BAR domains associated with the generation or maintenance of membrane curvature. The cell biology of these proteins remains less understood. Here, we initially confirm that EHD2, a protein previously shown biochemically to be present in caveolar fractions and to bind to pacsins, is a caveolar protein. We go on to report that GFP–pacsin 2 can be recruited to caveolae, and that endogenous pacsin 2 partially colocalises with caveolin 1 at the plasma membrane. Analysis of the role of pacsin 2 in caveolar biogenesis using small interfering RNA (siRNA) reveals that loss of pacsin 2 function results in loss of morphologically defined caveolae and accumulation of caveolin proteins within the plasma membrane. Overexpression of the F-BAR domain of pacsin 2 (but not the related F-BAR domains of CIP4 and FBP17) disrupts caveolar morphogenesis or trafficking, implying that pacsin 2 interacts with components required for these processes. We propose that pacsin 2 has an important role in the formation of plasma membrane caveolae.
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Doherty, G. J., & McMahon, H. T. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.081307.110540 · Cited by 3,075
A High Precision Survey of the Molecular Dynamics of Mammalian Clathrin-Mediated Endocytosis
Taylor, M. J., Perrais, D., & Merrifield, C. J. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1000604 · Cited by 754
Ultrastructural identification of uncoated caveolin-independent early endocytic vehicles
Kirkham, M., Fujita, A., Chadda, R., Nixon, S. J., Kurzchalia, T. V., Sharma, D. K., Pagano, R. E., Hancock, J. F., Mayor, S., & Parton, R. G. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200407078 · Cited by 439
Howes, M. T., Kirkham, M., Riches, J., Cortese, K., Walser, P. J., Simpson, F., Hill, M. M., Jones, A., Lundmark, R., Lindsay, M. R., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201002119 · Cited by 303
Molecular basis for SH3 domain regulation of F-BAR–mediated membrane deformation
Rao, Y., Ma, Q., Vahedi-Faridi, A., Sundborger, A., Pechstein, A., Puchkov, D., Luo, L., Shupliakov, O., Saenger, W., & Haucke, V. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1003478107 · Cited by 149
Cited by
Clathrin-independent pathways of endocytosis
Mayor, S., Parton, R. G., & Donaldson, J. G. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016758 · Cited by 525
The role of toxins in Clostridium difficile infection
Chandrasekaran, R., & Lacy, D. B. (2017) · FEMS Microbiology Reviews · doi:10.1093/femsre/fux048 · Cited by 353
Membrane curvature in cell biology: An integration of molecular mechanisms
Jarsch, I. K., Daste, F., & Gallop, J. L. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201604003 · Cited by 328
Caveolae: Structure, Function, and Relationship to Disease
Parton, R. G. (2018) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100617-062737 · Cited by 293
Cavin family proteins and the assembly of caveolae
Kovtun, O., Tillu, V. A., Ariotti, N., Parton, R. G., & Collins, B. M. (2015) · Journal of Cell Science · doi:10.1242/jcs.167866 · Cited by 230
Metadata
- Authors
- Hansen, C. G., Howard, G., & Nichols, B. J.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2011-08-15
- Volume
- 124
- Issue
- 16
- Pages
- 2777-2785
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2161703993
- Cited by
- 165
- References
- 5
- FWCI
- 4.22
- Type
- journal article
- Language
- en
- Open access
- closed
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