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Lindberg, Robert
Publications (2 of 2) Show all publications
Buch, C., Lindberg, R., Figueroa, R., Gudise, S., Onischenko, E. & Hallberg, E. (2009). An integral protein of the inner nuclear membrane localizes to the mitotic spindle in mammalian cells. Journal of Cell Science, 122(12), 2100-2107
Open this publication in new window or tab >>An integral protein of the inner nuclear membrane localizes to the mitotic spindle in mammalian cells
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2009 (English)In: Journal of Cell Science, ISSN 0021-9533, E-ISSN 1477-9137, Vol. 122, no 12, p. 2100-2107Article in journal (Refereed) Published
Abstract [en]

Here, we characterize a transmembrane protein of the nuclear envelope that we name spindle-associated membrane protein 1 (Samp1). The protein is conserved in metazoa and fission yeast and is homologous to Net5 in rat and Ima1 in Schizosaccharomyces pombe. We show that, in human cells, the protein is a membrane-spanning polypeptide with an apparent molecular mass of 43 kDa. This is consistent with a predicted polypeptide of 392 amino acids that has five transmembrane segments and its C-terminus exposed to the nucleoplasm. During interphase, Samp1 was specifically distributed in the inner nuclear membrane. Post-transcriptional silencing of Samp1 expression resulted in separation of centrosomes from the nuclear envelope, indicating that it is functionally connected to the cytoskeleton. At the onset of mitosis, most of the protein dispersed out into the ER, as expected. However, during mitosis, a significant fraction of the protein specifically localized to the polar regions of the mitotic spindle. We demonstrate for the first time, in human cells, the existence of a membranous structure overlapping with the mitotic spindle. Interestingly, another integral inner nuclear membrane protein, emerin, was absent from the spindle-associated membranes. Thus, Samp1 defines a specific membrane domain associated with the mitotic spindle.

National Category
Cell Biology
Identifiers
urn:nbn:se:sh:diva-13897 (URN)10.1242/jcs.047373 (DOI)000266634800018 ()2-s2.0-68949170696 (Scopus ID)
Note

Som manuskript i avhandling. As manuscript in dissertation.

Available from: 2011-12-14 Created: 2011-12-14 Last updated: 2017-12-08Bibliographically approved
Balogun, H. A., Vasconcelos, N.-M. -., Lindberg, R., Haeggström, M., Moll, K., Chen, Q., . . . Berzins, K. (2009). Immunogenicity and antigenic properties of Pf332-C231, a fragment of a non-repeat region of the Plasmodium falciparum antigen Pf332. Vaccine, 28(1), 90-97
Open this publication in new window or tab >>Immunogenicity and antigenic properties of Pf332-C231, a fragment of a non-repeat region of the Plasmodium falciparum antigen Pf332
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2009 (English)In: Vaccine, ISSN 0264-410X, E-ISSN 1873-2518, Vol. 28, no 1, p. 90-97Article in journal (Refereed) Published
Abstract [en]

Antigen Pf332, a megadalton protein has been shown to be associated with the membrane of infected erythrocytes Detailed functional studies on the antigen have remained hampered by the cross-reactive nature of antibodies generated to Pf332 PB32-C231, identified in the C-terminal region of Pf332 was cloned and antibodies against the C231 fragment were shown to react with intact Pf332 antigen by both immunofluorescence and immunoblotting analyses Antibodies to C231 inhibited in vitro Plasmodium falciparum growth efficiently In addition. human sera from malaria-exposed individuals reacted with recombinant C231 We show that Pf332-C231 represents a functional domain and is expected to facilitate further studies on Pf332 as a potential target for protective immune responses and the function of the antigen.

National Category
Immunology
Identifiers
urn:nbn:se:sh:diva-13873 (URN)10.1016/j.vaccine.2009.09.110 (DOI)000274869200012 ()19822232 (PubMedID)2-s2.0-70649086102 (Scopus ID)
Available from: 2011-12-14 Created: 2011-12-14 Last updated: 2017-12-08Bibliographically approved
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