sh.sePublications
Change search
Link to record
Permanent link

Direct link
Gudise, Santhosh
Publications (2 of 2) Show all publications
Figueroa, R., Gudise, S., Larsson, V. & Hallberg, E. (2010). A transmembrane inner nuclear membrane protein in the mitotic spindle. Nucleus, 1(3), 249-253
Open this publication in new window or tab >>A transmembrane inner nuclear membrane protein in the mitotic spindle
2010 (English)In: Nucleus, ISSN 1949-1042, Vol. 1, no 3, p. 249-253Article in journal (Refereed) Published
Abstract [en]

We have recently characterized a novel transmembrane protein of the inner nuclear membrane of mammalian cells. The protein has two very interesting features. First, despite being an integral membrane protein it is able to concentrate in the membranes colocalizing with the mitotic spindle in metaphase and anaphase. Hence, the protein was named Samp1, Spindle associated membrane protein 1. Secondly, it displays a functional connection to centrosomes. This article discusses various aspects of Samp1 in relation to possible cellular function(s).

National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:sh:diva-17499 (URN)10.4161/nucl.1.3.11740 (DOI)000208668400006 ()21327071 (PubMedID)2-s2.0-77957681891 (Scopus ID)
Available from: 2012-12-14 Created: 2012-12-14 Last updated: 2017-07-18Bibliographically approved
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
Show others...
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
Organisations

Search in DiVA

Show all publications