spn-F encodes a novel protein that affects oocyte patterning and bristle morphology in Drosophila.
نویسندگان
چکیده
The anteroposterior and dorsoventral axes of the Drosophila embryo are established during oogenesis through the activities of Gurken (Grk), a Tgfalpha-like protein, and the Epidermal growth factor receptor (Egfr). spn-F mutant females produce ventralized eggs similar to the phenotype produced by mutations in the grk-Egfr pathway. We found that the ventralization of the eggshell in spn-F mutants is due to defects in the localization and translation of grk mRNA during mid-oogenesis. Analysis of the microtubule network revealed defects in the organization of the microtubules around the oocyte nucleus. In addition, spn-F mutants have defective bristles. We cloned spn-F and found that it encodes a novel coiled-coil protein that localizes to the minus end of microtubules in the oocyte, and this localization requires the microtubule network and a Dynein heavy chain gene. We also show that Spn-F interacts directly with the Dynein light chain Ddlc-1. Our results show that we have identified a novel protein that affects oocyte axis determination and the organization of microtubules during Drosophila oogenesis.
منابع مشابه
A transport and retention mechanism for the sustained distal localization of Spn-F–IKKε during Drosophila bristle elongation
Stable localization of the signaling complex is essential for the robust morphogenesis of polarized cells. Cell elongation involves molecular signaling centers that coordinately regulate intracellular transport and cytoskeletal structures. In Drosophila bristle elongation, the protein kinase IKKε is activated at the distal tip of the growing bristle and regulates the shuttling movement of recyc...
متن کاملThe Drosophila spn-D gene encodes a RAD51C-like protein that is required exclusively during meiosis.
In Drosophila, mutations in double-strand DNA break (DSB) repair enzymes, such as spn-B, activate a meiotic checkpoint leading to dorsal-ventral patterning defects in the egg and an abnormal appearance of the oocyte nucleus. Mutations in spn-D cause an array of ovarian phenotypes similar to spn-B. We have cloned the spn-D locus and found that it encodes a protein of 271 amino acids that shows s...
متن کاملspindle-C (spn-C) and okra (okr), cause a delay in oocyte determination and a failure to accumulate Grk protein, leading to defects in AP and DV patterning in late oogenesis
Polarization of the anteroposterior (AP) axis of the Drosophila oocyte occurs early in oogenesis, while the presumptive oocyte is still in the germarium (Gonzalez-Reyes and St Johnston, 1998). The dorsoventral (DV) axis is set up much later and relies on transfer of the AP axis polarity from the oocyte to the somatic follicle cells at the posterior end of the oocyte. During stages 4-6 in wild-t...
متن کاملDev121863 1..14
Stable localization of the signaling complex is essential for the robust morphogenesis of polarized cells. Cell elongation involves molecular signaling centers that coordinately regulate intracellular transport and cytoskeletal structures. In Drosophila bristle elongation, the protein kinase IKKε is activated at the distal tip of the growing bristle and regulates the shuttling movement of recyc...
متن کاملDrosophila oocyte polarity and cytoskeleton organization require regulation of Ik2 activity by Spn-F and Javelin-like.
The Drosophila melanogaster Spn-F, Ik2, and Javelin-like (Jvl) proteins interact to regulate oocyte mRNA localization and cytoskeleton organization. However, the mechanism by which these proteins interact remains unclear. Using antibodies to activated Ik2, we showed that this protein is found at the region of oocyte and follicle cell where microtubule minus ends are enriched. We demonstrate tha...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Development
دوره 133 8 شماره
صفحات -
تاریخ انتشار 2006