Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Echinobase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
Echinobase
ECB-ART-36537
J Cell Biol 1996 Dec 01;1356 Pt 2:1715-25. doi: 10.1083/jcb.135.6.1715.
Show Gene links Show Anatomy links

Targeting of membranes to sea urchin sperm chromatin is mediated by a lamin B receptor-like integral membrane protein.

Collas P , Courvalin JC , Poccia D .


???displayArticle.abstract???
We have identified an integral membrane protein of sea urchin gametes with an apparent molecular mass of 56 kD that cross-reacts with an antibody against the nucleoplasmic NH2-terminal domain of human lamin B receptor (LBR). In mature sperm, p56 is located at the tip and base of the nucleus from where it is removed by egg cytosol in vitro. In the egg, p56 is present in a subset of cytoplasmic membranes (MV2 beta) which contributes the bulk of the nuclear envelope during male pronuclear formation. p56-containing vesicles are required for nuclear envelope assembly and have a chromatin-binding capacity that is mediated by p56. Lamin B is not present in these vesicles and is imported into the nucleus from a soluble pool at a later stage of pronuclear formation. Lamin B incorporation and addition of new membranes are necessary for pronuclear swelling and nuclear envelope growth. We suggest that p56 is a sea urchin LBR homologue that targets membranes to chromatin and later anchors the membrane to the lamina.

???displayArticle.pubmedLink??? 8991085
???displayArticle.pmcLink??? PMC2133942
???displayArticle.link??? J Cell Biol


Genes referenced: LOC100887844 LOC105444438 LOC576396 mpp5
???displayArticle.antibodies??? LOC373247 Ab4

References [+] :
Aebi, The nuclear lamina is a meshwork of intermediate-type filaments. 1986, Pubmed