ArticleThe Journal of cell biology1997
A small conserved domain in the yeast Spa2p is necessary and sufficient for its polarized localization.
Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
33 citing papers in PubMed.
- A positive feedback loop involving the Spa2 SHD domain contributes to focal polarization.PloS one · 2022Article
- Chemotactic movement of a polarity site enables yeast cells to find their mates.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Type V myosin focuses the polarisome and shapes the tip of yeast cells.The Journal of cell biology · 2021Article
- The shared role of the Rsr1 GTPase and Gic1/Gic2 in Cdc42 polarization.Molecular biology of the cell · 2018Article
- Cell polarity protein Spa2 coordinates Chs2 incorporation at the division site in budding yeast.PLoS genetics · 2018Article
- Evolutionary dynamics in the fungal polarization network, a mechanistic perspective.Biophysical reviews · 2017Review
- Alternative cell polarity behaviours arise from changes in G-protein spatial dynamics.IET systems biology · 2015Article
- Fertility and polarized cell growth depends on eIF5A for translation of polyproline-rich formins in Saccharomyces cerevisiae.Genetics · 2014Article
- Yeast G-proteins mediate directional sensing and polarization behaviors in response to changes in pheromone gradient direction.Molecular biology of the cell · 2013Article
- Spatial stochastic dynamics enable robust cell polarization.PLoS computational biology · 2013Article
- Cdc42p regulation of the yeast formin Bni1p mediated by the effector Gic2p.Molecular biology of the cell · 2012Article
- Phosphorylation of GIT1 tyrosine 321 is required for association with FAK at focal adhesions and for PDGF-activated migration of osteoblasts.Molecular and cellular biochemistry · 2012Article
- Initial polarized bud growth by endocytic recycling in the absence of actin cable-dependent vesicle transport in yeast.Molecular biology of the cell · 2010Article
- Chemical gradients and chemotropism in yeast.Cold Spring Harbor perspectives in biology · 2009Review
- Article
- Inheritance of cortical ER in yeast is required for normal septin organization.The Journal of cell biology · 2007Article
- The yeast actin cytoskeleton: from cellular function to biochemical mechanism.Microbiology and molecular biology reviews : MMBR · 2006Review
- Cdc42p GDP/GTP cycling is necessary for efficient cell fusion during yeast mating.Molecular biology of the cell · 2006Article
- Regulation of cell polarity by interactions of Msb3 and Msb4 with Cdc42 and polarisome components.Molecular and cellular biology · 2005Article
- Cell polarity protein Spa2P associates with proteins involved in actin function in Saccharomyces cerevisiae.Molecular biology of the cell · 2005Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SPA2 encodes a yeast protein that is one of the first proteins to localize to sites of polarized growth, such as the shmoo tip and the incipient bud. The dynamics and requirements for Spa2p localization in living cells are examined using Spa2p green fluorescent protein fusions. Spa2p localizes to one edge of unbudded cells and subsequently is observable in the bud tip. Finally, during cytokinesis Spa2p is present as a ring at the mother-daughter bud neck. The bud emergence mutants bem1 and bem2 and mutants defective in the septins do not affect Spa2p localization to the bud tip. Strikingly, a small domain of Spa2p comprised of 150 amino acids is necessary and sufficient for localization to sites of polarized growth. This localization domain and the amino terminus of Spa2p are essential for its function in mating. Searching the yeast genome database revealed a previously uncharacterized protein which we name, Sph1p (a2p omolog), with significant homology to the localization domain and amino terminus of Spa2p. This protein also localizes to sites of polarized growth in budding and mating cells. SPH1, which is similar to SPA2, is required for bipolar budding and plays a role in shmoo formation. Overexpression of either Spa2p or Sph1p can block the localization of either protein fused to green fluorescent protein, suggesting that both Spa2p and Sph1p bind to and are localized by the same component. The identification of a 150-amino acid domain necessary and sufficient for localization of Spa2p to sites of polarized growth and the existence of this domain in another yeast protein Sph1p suggest that the early localization of these proteins may be mediated by a receptor that recognizes this small domain.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.