The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The requested protein is correctly identified as WPP domain-interacting protein 1 (AtWIP1), locus At4g26455, UniProt Q8GXA4, from Arabidopsis thaliana. It is a plant-specific, tail-anchored outer nuclear membrane (ONM) KASH-like protein and a component of plant LINC-related nuclear-envelope assemblies. It is not an enzyme or transporter: its primary function is to act as a membrane anchor and protein-interaction scaffold linking inner-nuclear-membrane SUN proteins to cytoplasmic RanGAP- and WIT/myosin-associated machinery. This architecture supports RanGAP localization, nuclear morphology and movement, and—collectively with WIP2 and WIP3—pollen vegetative-nucleus positioning and male fertility. (groves2020recentadvancesin pages 2-3, zhou2012novelplantsun–kash pages 5-6, zhou2013howplantslinc pages 3-5)
The strongest functional phenotypes generally derive from wip1 wip2 wip3 or larger higher-order mutants. Consequently, family-level phenotypes should not be attributed uniquely to AtWIP1; substantial paralog redundancy is a central annotation constraint. (zhou2015plantnuclearshape pages 3-4, zhou2012novelplantsun–kash pages 5-6)
The literature explicitly maps WIP1 to At4g26455 and classifies it with Arabidopsis WIP2 and WIP3 as a WPP domain-interacting/KASH-protein group localized to the nuclear envelope and ER. This matches the supplied UniProt identity, organism, and WIP1/2/3 and WIP coiled-coil domain assignments. (groves2020recentadvancesin pages 2-3)
The symbol is highly ambiguous. This report excludes:
Those proteins have different domains, localization, and biochemical functions. The decisive identifiers here are At4g26455/Q8GXA4, “WPP domain-interacting protein 1,” and the nuclear-envelope KASH-like architecture.
AtWIP1 is a single-pass, tail-anchored membrane protein. Its long N-terminal region faces the cytoplasm and contains coiled-coil interaction capacity; a near-C-terminal transmembrane segment anchors it in the ONM, while a short C-terminal tail projects into the perinuclear space. That tail ends in a plant-conserved VVPT/VPT motif, functionally analogous to the terminal KASH motif of opisthokont KASH proteins. Immunofluorescence and immunogold evidence support ONM placement. (zhou2012novelplantsun–kash pages 4-4, zhou2012novelplantsun–kash pages 3-4, zhou2013howplantslinc pages 3-5)
Accordingly, WIP1’s primary biochemical function is structural/adaptor-like rather than catalytic. No catalytic reaction, active site, metabolite substrate, transported solute, or channel activity is established. Its function is defined by protein binding on opposite sides of the ONM:
GFP-WIP1 is enriched at the nuclear envelope, specifically the ONM, which is continuous with the endoplasmic reticulum. Reviews therefore annotate its distribution as NE/ER rather than as a freely soluble nuclear protein. (groves2020recentadvancesin pages 2-3, zhou2013howplantslinc pages 3-5)
Localization is mechanistically dependent on SUN binding. In wild-type roots, GFP-WIP1 showed strong NE enrichment, whereas deletion of its terminal VVPT sequence or reduction of SUN1/SUN2 function shifted signal toward a diffuse cytoplasmic/ER distribution. The difference in nuclear-envelope localization index was significant at P < 0.01 with n = 50 cells. These results indicate that the transmembrane segment inserts WIP1 into the membrane system, while SUN–VVPT binding selectively retains or concentrates it at the nuclear envelope. (zhou2012novelplantsun–kash pages 4-5, zhou2012novelplantsun–kash pages 4-4)
FRAP experiments further showed that WIP1 mobility decreases when SUN1 or SUN2 is present. Deleting VVPT abolishes this SUN-dependent immobilization. Co-immunoprecipitation mapped the interaction to the SUN domain of SUN2 and the C-terminal region of WIP1. (zhou2012novelplantsun–kash pages 4-4, zhou2012novelplantsun–kash pages 3-4)
AtWIP1 interacts directly with both SUN1 and SUN2. SUN proteins reside in the inner nuclear membrane, while WIP1 resides in the ONM; their association across the perinuclear lumen forms a plant SUN–KASH bridge. This is the core structural basis for assigning WIP1 to a plant LINC-related complex. (zhou2012novelplantsun–kash pages 4-4, zhou2012novelplantsun–kash pages 3-4, zhou2012novelplantsun–kash pages 1-2)
The cytoplasmic coiled-coil region of WIP1 binds the N-terminal WPP domain of Arabidopsis RanGAP1. Co-immunoprecipitation showed that SUN2 associates with RanGAP1 only when WIP1 is coexpressed, supporting the arrangement SUN2–WIP1–RanGAP1, with WIP1 bridging the luminal SUN protein and cytoplasmic RanGAP. (zhou2012novelplantsun–kash pages 5-6)
RanGAP1-GFP becomes significantly more diffuse in both the wip1 wip2 wip3 and SUN-deficient backgrounds (P < 0.01; n = 55), demonstrating that SUN–WIP assemblies are required for normal RanGAP concentration at the NE. This role is important to plant nuclear organization because plants lack the canonical opisthokont RanGAP anchoring mechanism and instead use the plant-specific WPP–WIP system. (zhou2012novelplantsun–kash pages 4-5, zhou2013howplantslinc pages 3-5)
WIP proteins also associate with WIT1/WIT2 at the ONM. WIT2 binds myosin XI-i, generating a proposed SUN–WIP–WIT2–myosin XI-i mechanical pathway. Co-immunoprecipitation and mutant-localization experiments show that WIT2 and SUN proteins contribute to recruitment of the myosin XI-i tail at the NE. This complex provides a plausible route by which actomyosin-generated cytoplasmic forces are transmitted to the nucleus. (zhou2015plantnuclearshape pages 3-4, zhou2015plantnuclearshape pages 4-5)
The most precise pathway assignment is therefore:
nucleoskeleton/inner nuclear membrane → SUN1/SUN2 → WIP1/2/3 in the ONM → WIT proteins → myosin XI-i/actin, with a parallel cytoplasmic WIP interaction anchoring RanGAP at the envelope.
SUN–WIP bridges contribute to the elongated morphology characteristic of differentiated Arabidopsis epidermal and trichome nuclei. The wip1 wip2 wip3 triple mutant has significantly rounder nuclei, as do SUN1/SUN2-deficient plants. Nuclear morphology was assessed by width:length ratio or circularity, with reported samples including 60 leaf epidermal nuclei, 20 trichome nuclei, and 55 root-hair nuclei. (zhou2012novelplantsun–kash pages 5-6, zhou2012novelplantsun–kash pages 1-2)
Pairwise WIP double mutants also showed increased trichome-nucleus circularity, supporting overlapping contributions by WIP1, WIP2, and WIP3 rather than a uniquely dominant WIP1 role. WIP1 itself remained substantially NE-localized in a crwn1 background, indicating that its envelope association does not require CRWN1 and that the SUN–WIP pathway and nucleoplasmic CRWN pathway make partly independent contributions to nuclear shape. (zhou2015plantnuclearshape pages 3-4, zhou2015plantnuclearshape pages 4-5)
Through WIT/myosin coupling, the WIP-containing bridge participates in nuclear movement. Mutations affecting the SUN–WIP–WIT/myosin system impair nuclear movement in differentiated tissues and alter nuclear morphology. The likely mechanical interpretation is that ONM WIP complexes transmit actomyosin force to the nuclear envelope rather than catalyzing a signaling reaction. (zhou2015plantnuclearshape pages 4-5, zhou2015plantnuclearshape pages 7-8)
During pollen-tube growth, the vegetative nucleus normally precedes the two sperm cells and maintains an appropriate position relative to the growing tip. Loss of all three WIPs reverses vegetative-nucleus/sperm-cell order and frequently causes loss of the vegetative nucleus from the advancing male germ unit. These defects are associated with failed ovular targeting or reception, pollen-tube overgrowth, polytubey, seed loss, and reduced male fertility. (zhou2015sunanchorspollen pages 1-2)
A dominant SUN construct that competes for KASH binding displaced GFP-WIP1 and GFP-WIT1 from the vegetative nuclear envelope and produced vegetative-nucleus movement and fertility defects. This supplies mechanistic evidence that SUN-mediated retention of the WIP–WIT complex—not merely WIP expression—is required in pollen. (zhou2015sunanchorspollen pages 7-8)
These reproductive findings are biologically important but are principally WIP-family-level evidence. They do not demonstrate that loss of WIP1 alone is sufficient to generate the full phenotype.
| Annotation aspect | Best-supported conclusion | Evidence type / method | Gene-specific vs. family-level status | Key source, date, and DOI URL |
|---|---|---|---|---|
| Identity and ambiguity warning | The target is Arabidopsis thaliana At4g26455, UniProt Q8GXA4, encoding nuclear-envelope WPP domain-interacting protein 1 (AtWIP1). It must not be conflated with the unrelated plant C2H2 zinc-finger WIP/TT1 transcription factors or mammalian PPM1D/WIP1 phosphatase. | Locus mapping and nuclear-envelope protein classification | Gene-specific identity; ambiguity resolved by locus/accession | Groves et al., Jan. 2020, 10.1080/19491034.2020.1846836 (groves2020recentadvancesin pages 2-3) |
| Architecture and topology | WIP1 is a plant-specific, tail-anchored KASH-like protein with a long cytoplasmic N-terminal region containing coiled-coil structure, a near-C-terminal transmembrane anchor, and a short tail in the perinuclear space ending in the conserved VVPT/VPT motif. This agrees with the WIP coiled-coil domains assigned to Q8GXA4. | Sequence comparison, truncation/deletion constructs, topology analysis, immunolocalization | Architecture supported for WIP1 directly and conserved across WIP1–WIP3 | Zhou & Meier, May 2013, 10.4161/nucl.24088 (zhou2013howplantslinc pages 3-5); Zhou et al., Jan. 2012, 10.1083/jcb.201108098 (zhou2012novelplantsun–kash pages 4-4, zhou2012novelplantsun–kash pages 3-4) |
| Cellular localization | GFP-WIP1 is enriched at the outer nuclear membrane (ONM), continuous with the ER; reviews accordingly annotate WIP1 as NE/ER-associated. The bulk N terminus faces the cytoplasm, while the short C-terminal tail enters the perinuclear lumen. | GFP imaging, immunofluorescence, immunogold localization, topology inference | Direct WIP1 localization plus family-level ultrastructural support | Zhou & Meier, May 2013, 10.4161/nucl.24088 (zhou2013howplantslinc pages 3-5); Groves et al., Jan. 2020, 10.1080/19491034.2020.1846836 (groves2020recentadvancesin pages 2-3) |
| SUN1/SUN2 interaction | WIP1 binds the SUN-domain proteins SUN1 and SUN2 across the nuclear envelope. SUN interaction requires the SUN domain and WIP1’s C-terminal KASH-like region, including VVPT. | Co-immunoprecipitation and FRAP mobility assays with full-length and deletion constructs | Directly demonstrated for WIP1 | Zhou et al., Jan. 2012, 10.1083/jcb.201108098 (zhou2012novelplantsun–kash pages 4-4, zhou2012novelplantsun–kash pages 3-4) |
| SUN-dependent retention | Deleting WIP1’s terminal VVPT motif or reducing SUN1/SUN2 function shifts GFP-WIP1 from strong NE enrichment toward diffuse cytoplasmic/ER signal. NE-localization-index differences were significant (P < 0.01; n = 50), showing that SUN binding retains WIP1 at the NE rather than merely inserting it into membrane. | Quantitative fluorescence imaging and NE-localization index; deletion and mutant analysis | Directly demonstrated for WIP1 | Zhou et al., Jan. 2012, 10.1083/jcb.201108098 (zhou2012novelplantsun–kash pages 4-5, zhou2012novelplantsun–kash pages 4-4) |
| RanGAP1 anchoring | WIP1’s cytoplasmic coiled-coil region binds the N-terminal WPP domain of RanGAP1, anchoring RanGAP at the NE. SUN2 co-precipitates with RanGAP1 only when WIP1 is present, placing WIP1 between luminal SUN and cytoplasmic RanGAP. RanGAP1 becomes more diffuse in the wip1 wip2 wip3 and SUN-deficient backgrounds (P < 0.01; n = 55). | Co-immunoprecipitation, domain mapping, GFP localization, quantitative mutant imaging | WIP1 binding is direct; physiological anchorage is redundantly mediated by WIP1–WIP3 | Zhou et al., Jan. 2012, 10.1083/jcb.201108098 (zhou2012novelplantsun–kash pages 5-6, zhou2012novelplantsun–kash pages 4-5); Zhou & Meier, May 2013, 10.4161/nucl.24088 (zhou2013howplantslinc pages 3-5) |
| WIT2–myosin XI-i linkage | WIP proteins associate with WIT proteins at the ONM; WIT2 in turn binds myosin XI-i. The resulting SUN–WIP–WIT2–myosin XI-i assembly provides a mechanical link from the nuclear interior/INM to a cytoplasmic actomyosin motor. The available evidence does not establish that WIP1 alone is the uniquely required paralog. | Co-immunoprecipitation in Nicotiana benthamiana, fluorescent localization, mutant-dependent recruitment | WIP-family-level mechanical function; WIP1 was among directly tested WIT-binding proteins | Zhou et al., Mar. 2015, 10.1080/19491034.2014.1003512 (zhou2015plantnuclearshape pages 3-4, zhou2015plantnuclearshape pages 4-5) |
| Nuclear-shape function | SUN–WIP bridges help maintain elongated nuclei in differentiated epidermal cells and trichomes. The wip1 wip2 wip3 triple mutant has rounder, less elongated nuclei; pairwise WIP double mutants also increase trichome nuclear circularity, supporting overlapping paralog functions. | Higher-order loss-of-function genetics and quantitative width:length or circularity measurements; reported samples included leaf epidermis n = 60, trichomes n = 20, and root hairs n = 55 | Predominantly WIP-family-level because redundancy obscures WIP1-specific contribution | Zhou et al., Jan. 2012, 10.1083/jcb.201108098 (zhou2012novelplantsun–kash pages 5-6); Zhou et al., Mar. 2015, 10.1080/19491034.2014.1003512 (zhou2015plantnuclearshape pages 3-4) |
| Pollen vegetative-nucleus movement and fertility | WIP-containing LINC complexes retain and move the vegetative nucleus during pollen-tube growth. Triple WIP loss reverses vegetative-nucleus/sperm-cell order, promotes vegetative-nucleus loss, and impairs pollen-tube guidance/reception, producing overgrown tubes, polytubey, seed loss, and reduced male fertility. Dominant disruption of SUN–KASH interaction displaces GFP-WIP1 from the vegetative nuclear envelope and reproduces movement/fertility defects. | Triple-mutant genetics, pollen-tube live imaging, dominant-negative SUN constructs, ovular targeting/reception and seed-set assays | Strong family-level requirement; WIP1 localization is direct, but a unique WIP1-only reproductive requirement is not established | Zhou et al., Sept. 2015, 10.1093/jxb/erv425 (zhou2015sunanchorspollen pages 1-2, zhou2015sunanchorspollen pages 7-8) |
| Redundancy caveat | WIP1, WIP2, and WIP3 are substantially redundant. Strong phenotypes generally require pairwise or triple disruption, so phenotypes of wip123 or broader wifi mutants cannot be assigned solely to At4g26455. A weak or absent single-wip1 phenotype does not imply that WIP1 lacks molecular activity. | Comparison of single, double, triple, and higher-order mutant combinations | Essential interpretive limitation | Zhou et al., Jan. 2012, 10.1083/jcb.201108098 (zhou2012novelplantsun–kash pages 5-6, zhou2012novelplantsun–kash pages 1-2); Zhou et al., Mar. 2015, 10.1080/19491034.2014.1003512 (zhou2015plantnuclearshape pages 3-4) |
| Biochemical classification | WIP1 is a structural adaptor/ membrane anchor, not an enzyme or transporter. No catalytic reaction, active site, metabolite substrate, or transported solute is known. Its molecular “substrates” are protein partners: SUN1/2, RanGAP, and WIT-containing assemblies. | Domain architecture, interaction mapping, and absence of catalytic-domain evidence | Gene- and family-level conclusion | Zhou et al., Jan. 2012, 10.1083/jcb.201108098 (zhou2012novelplantsun–kash pages 5-6, zhou2012novelplantsun–kash pages 3-4); Groves et al., Jan. 2020, 10.1080/19491034.2020.1846836 (groves2020recentadvancesin pages 2-3) |
| 2023–2024 evidence status | No 2023–2024 primary study focused specifically on AtWIP1/At4g26455 was identified in the searched literature. A 2024 wheat study supports evolutionary conservation of a SUN–WIP nuclear-membrane interaction, but it is comparative ortholog evidence and cannot replace direct Arabidopsis data. | Targeted literature search; comparative localization and interaction assays in wheat | Evidence-gap statement; 2024 result is not AtWIP1-specific | Guo et al., June 2024, 10.1007/s44154-024-00163-z (guo2024identificationofnuclear pages 9-11) |
Table: Evidence summary for the correctly identified Arabidopsis nuclear-envelope WIP1, separating direct AtWIP1 findings from redundant WIP-family phenotypes. It highlights molecular architecture, localization, interactions, biological roles, and key annotation limitations.
The direct, WIP1-specific evidence is strongest for:
By contrast, the clearest developmental and cellular phenotypes rely on double, triple, or higher-order mutants. Therefore, the most defensible wording is that WIP1 contributes redundantly with WIP2 and WIP3 to RanGAP anchoring, nuclear morphology, nuclear movement, pollen-tube organization, and male fertility. A weak or absent single-wip1 phenotype should not be interpreted as absence of molecular function. (zhou2015plantnuclearshape pages 3-4, zhou2012novelplantsun–kash pages 5-6)
No 2023–2024 primary publication focused specifically on Arabidopsis AtWIP1/At4g26455 was identified in the searched literature. The molecular annotation consequently remains anchored in the rigorous 2012–2015 interaction, imaging, and genetics studies. A 2020 authoritative review continued to classify At4g26455 as a NE/ER-localized KASH protein associated with SUN and WIT partners. (groves2020recentadvancesin pages 2-3)
A 2024 wheat study identified a nuclear-membrane TaWIP1 ortholog and supported SUN–WIP interaction and conserved WIP/WIT/WPP organization under fungal-stress conditions. This is useful evolutionary corroboration, but it is not direct evidence for a new AtWIP1 function and should not be used to infer pathogen-response phenotypes for At4g26455 without Arabidopsis experiments. (guo2024identificationofnuclear pages 9-11)
In practical research, WIP-derived ONM-targeting modules have value for nuclear-envelope labeling and affinity-based nucleus-isolation technologies. Such engineering applications exploit the reliable membrane anchoring of WIP proteins; they do not establish an additional native enzymatic function for AtWIP1.
AtWIP1 (At4g26455/Q8GXA4) is a plant-specific, tail-anchored outer nuclear membrane KASH-like adaptor. Its C-terminal VVPT-containing perinuclear tail binds SUN1/SUN2 and retains it at the nuclear envelope, while its cytoplasmic coiled-coil region binds WPP-domain RanGAP and participates in WIT–myosin XI-i assemblies. Together with the redundant paralogs WIP2 and WIP3, it anchors RanGAP, contributes to nuclear shape and actomyosin-dependent nuclear positioning, and supports vegetative-nucleus movement and efficient male fertility during pollen-tube growth. It has no established catalytic or transport activity. (zhou2015sunanchorspollen pages 1-2, zhou2012novelplantsun–kash pages 5-6, zhou2012novelplantsun–kash pages 3-4, zhou2013howplantslinc pages 3-5)
References
(groves2020recentadvancesin pages 2-3): Norman Reid Groves, Alecia Biel, Morgan Moser, Tyler Mendes, Katelyn Amstutz, and Iris Meier. Recent advances in understanding the biological roles of the plant nuclear envelope. Nucleus, 11:330-346, Jan 2020. URL: https://doi.org/10.1080/19491034.2020.1846836, doi:10.1080/19491034.2020.1846836. This article has 23 citations and is from a peer-reviewed journal.
(zhou2012novelplantsun–kash pages 5-6): Xiao Zhou, Katja Graumann, David E. Evans, and Iris Meier. Novel plant sun–kash bridges are involved in rangap anchoring and nuclear shape determination. The Journal of Cell Biology, 196:203-211, Jan 2012. URL: https://doi.org/10.1083/jcb.201108098, doi:10.1083/jcb.201108098. This article has 188 citations.
(zhou2013howplantslinc pages 3-5): Xiao Zhou and Iris Meier. How plants linc the sun to kash. Nucleus, 4:206-215, May 2013. URL: https://doi.org/10.4161/nucl.24088, doi:10.4161/nucl.24088. This article has 65 citations and is from a peer-reviewed journal.
(zhou2015plantnuclearshape pages 3-4): Xiao Zhou, Norman Reid Groves, and Iris Meier. Plant nuclear shape is independently determined by the sun-wip-wit2-myosin xi-i complex and crwn1. Nucleus, 6:144-153, Mar 2015. URL: https://doi.org/10.1080/19491034.2014.1003512, doi:10.1080/19491034.2014.1003512. This article has 74 citations and is from a peer-reviewed journal.
(zhou2012novelplantsun–kash pages 4-4): Xiao Zhou, Katja Graumann, David E. Evans, and Iris Meier. Novel plant sun–kash bridges are involved in rangap anchoring and nuclear shape determination. The Journal of Cell Biology, 196:203-211, Jan 2012. URL: https://doi.org/10.1083/jcb.201108098, doi:10.1083/jcb.201108098. This article has 188 citations.
(zhou2012novelplantsun–kash pages 3-4): Xiao Zhou, Katja Graumann, David E. Evans, and Iris Meier. Novel plant sun–kash bridges are involved in rangap anchoring and nuclear shape determination. The Journal of Cell Biology, 196:203-211, Jan 2012. URL: https://doi.org/10.1083/jcb.201108098, doi:10.1083/jcb.201108098. This article has 188 citations.
(zhou2012novelplantsun–kash pages 4-5): Xiao Zhou, Katja Graumann, David E. Evans, and Iris Meier. Novel plant sun–kash bridges are involved in rangap anchoring and nuclear shape determination. The Journal of Cell Biology, 196:203-211, Jan 2012. URL: https://doi.org/10.1083/jcb.201108098, doi:10.1083/jcb.201108098. This article has 188 citations.
(zhou2012novelplantsun–kash pages 1-2): Xiao Zhou, Katja Graumann, David E. Evans, and Iris Meier. Novel plant sun–kash bridges are involved in rangap anchoring and nuclear shape determination. The Journal of Cell Biology, 196:203-211, Jan 2012. URL: https://doi.org/10.1083/jcb.201108098, doi:10.1083/jcb.201108098. This article has 188 citations.
(zhou2015plantnuclearshape pages 4-5): Xiao Zhou, Norman Reid Groves, and Iris Meier. Plant nuclear shape is independently determined by the sun-wip-wit2-myosin xi-i complex and crwn1. Nucleus, 6:144-153, Mar 2015. URL: https://doi.org/10.1080/19491034.2014.1003512, doi:10.1080/19491034.2014.1003512. This article has 74 citations and is from a peer-reviewed journal.
(zhou2015plantnuclearshape pages 7-8): Xiao Zhou, Norman Reid Groves, and Iris Meier. Plant nuclear shape is independently determined by the sun-wip-wit2-myosin xi-i complex and crwn1. Nucleus, 6:144-153, Mar 2015. URL: https://doi.org/10.1080/19491034.2014.1003512, doi:10.1080/19491034.2014.1003512. This article has 74 citations and is from a peer-reviewed journal.
(zhou2015sunanchorspollen pages 1-2): Xiao Zhou, Norman Reid Groves, and Iris Meier. Sun anchors pollen wip–wit complexes at the vegetative nuclear envelope and is necessary for pollen tube targeting and fertility. Journal of Experimental Botany, 66:7299-7307, Sep 2015. URL: https://doi.org/10.1093/jxb/erv425, doi:10.1093/jxb/erv425. This article has 51 citations and is from a domain leading peer-reviewed journal.
(zhou2015sunanchorspollen pages 7-8): Xiao Zhou, Norman Reid Groves, and Iris Meier. Sun anchors pollen wip–wit complexes at the vegetative nuclear envelope and is necessary for pollen tube targeting and fertility. Journal of Experimental Botany, 66:7299-7307, Sep 2015. URL: https://doi.org/10.1093/jxb/erv425, doi:10.1093/jxb/erv425. This article has 51 citations and is from a domain leading peer-reviewed journal.
(guo2024identificationofnuclear pages 9-11): Huan Guo, Jianfeng Wang, Di Yao, Ligang Yu, Wenting Jiang, Lincai Xie, Shikai Lv, Xiangyu Zhang, Yajuan Wang, Changyou Wang, Wanquan Ji, and Hong Zhang. Identification of nuclear membrane sun proteins and components associated with wheat fungal stress responses. Stress Biology, Jun 2024. URL: https://doi.org/10.1007/s44154-024-00163-z, doi:10.1007/s44154-024-00163-z. This article has 1 citations.