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  Maturation induced internalization of β1-integrin by Xenopus oocytes and formation of the maternal integrin pool

Müller, A., Gawantka, V., Ding, X., & Hausen, P. (1993). Maturation induced internalization of β1-integrin by Xenopus oocytes and formation of the maternal integrin pool. Mechanisms of Development, 42(1-2), 77-88. doi:10.1016/0925-4773(93)90100-c.

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 Creators:
Müller, AHJ1, Author                 
Gawantka, V1, Author           
Ding, X1, Author           
Hausen, P1, Author           
Affiliations:
1Department Cell Biology, Max Planck Institute for Developmental Biology, Max Planck Society, ou_3375717              

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 Abstract: A pool of beta 1-integrin, ready to be inserted into the cleavage membranes, is present in the cytoplasm of the Xenopus egg, while its plasma membrane is devoid of this membrane protein (Gawantka et al., 1992). The underlying mechanisms that lead to this specific pattern of beta 1-integrin distribution in the egg have been investigated. beta 1-Integrin is present on the oocyte membrane throughout oogenesis. During maturation the oocyte membrane is cleared of beta 1-integrin via internalization of the protein by the oocyte. Synthesis of beta 1-integrin precursor is stimulated moderately in the maturing oocyte. At the same time processing of the precursor into the mature form of beta 1-integrin and its complexing with a putative alpha-chain is greatly accelerated. This way a maternal integrin pool accumulates in the mature oocyte. It is localized in conspicuous yolk free patches which contain large amounts of endoplasmic reticulum, Golgi complexes and smooth vesicles. We suggest that membrane vesicles harbouring the beta 1-integrin are generated in these cytoplasmic regions and that this store of vesicles provides the material source for the rapid membrane formation during cleavage.

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 Dates: 1993-07
 Publication Status: Issued
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 Rev. Type: -
 Identifiers: DOI: 10.1016/0925-4773(93)90100-c
PMID: 7690240
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Title: Mechanisms of Development
Source Genre: Journal
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Publ. Info: Shannon : Elsevier
Pages: - Volume / Issue: 42 (1-2) Sequence Number: - Start / End Page: 77 - 88 Identifier: ISSN: 0925-4773
CoNE: https://pure.mpg.de/cone/journals/resource/954927703126